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2 ATP + 2 L-glutamate + 2 NH3
2 ADP + 2 phosphate + D-glutamine + D-isoglutamine
ADP + L-glutamine + hydroxylamine
gamma-glutamylhydroxamate + ?
ADP + phosphate + L-glutamine
ATP + L-glutamate + NH3
ATP + 3-aminopentanedioate + hydroxylamine
ADP + phosphate + ?
ATP + 3-aminopentanedioate + hydroxylamine
ADP + phosphate + gamma-glutamylhydroxamate
the enzyme is more selective for L-glutamate (alpha-glutamate) than 3-aminopentanedioate (beta-glutamate) as a substrate
-
-
?
ATP + adipate + NH4+
ADP + phosphate + ?
ATP + gamma-aminobutyrate + NH4+
ADP + phosphate + ?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
ATP + L-Glu + ethylamine
ADP + phosphate + ?
ATP + L-Glu + ethylamine
ADP + phosphate + L-Gln + ?
ATP + L-Glu + hydroxylamine
ADP + phosphate + gamma-glutamyl hydroxamate
ATP + L-Glu + hydroxylamine
ADP + phosphate + L-Gln + ?
ATP + L-Glu + methylamine
ADP + phosphate + ?
ATP + L-Glu + methylamine
ADP + phosphate + L-Gln + ?
-
7% of the activity with NH4+, at pH 8.0, activated with 30 mM Mg2+
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
ATP + L-glutamate + hydroxylamine
?
ATP + L-glutamate + hydroxylamine
ADP + phosphate + gamma-glutamyl hydroxamate
ATP + L-glutamate + hydroxylamine
ADP + phosphate + gamma-L-glutamyl hydroxamate
-
in presence of Mn2+
-
-
?
ATP + L-glutamate + hydroxylamine
ADP + phosphate + gamma-L-glutamylhydroxamate
ATP + L-glutamate + hydroxylamine
ADP + phosphate + L-gamma-glutamylhydroxamate
-
photometric determination of GS activity based on formation of an L-gamma-glutamylhydroxamate ferric chloride complex using hydroxylamine instead of ammonia
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
ATP + L-glutamate + NH4+
ADP + phosphate + L-glutamine
ATP + pentanedioate + NH4+
ADP + phosphate + ?
Gln + hydroxylamine + ADP
gamma-Glutamylhydroxamate + NH4+ + ?
GTP + L-Glu + NH4+
GDP + phosphate + L-Gln
hydroxylamine + L-glutamine + ATP
L-gamma-glutamyl-hydroxamate + ammonia + ADP
hydroxylamine + L-glutamine + ATP
L-gamma-glutamyl-hydroxamate + ammonium + ADP
ITP + L-Glu + NH4+
IDP + phosphate + L-Gln
L-Gln + hydroxylamine + ADP
gamma-glutamylhydroxamate + NH4+ + ?
L-Gln + hydroxylamine + ADP
L-gamma-glutamylhydroxamate + NH4+ + ?
-
-
-
?
L-glutamine + hydroxylamine + ADP
gamma-glutamylhydroxamate + NH3 + ?
-
partial reverse reaction
-
-
?
L-glutamine + hydroxylamine + ADP
gamma-glutamylhydroxamate + NH4+ + ?
TTP + L-Glu + NH4+
TDP + phosphate + L-Gln
-
10% of the activity relative to ATP
-
-
?
UTP + L-Glu + NH4+
UDP + phosphate + L-Gln
additional information
?
-
2 ATP + 2 L-glutamate + 2 NH3
2 ADP + 2 phosphate + D-glutamine + D-isoglutamine
GlnA2 catalyses the synthesis of D-glutamine and D-isoglutamine and is essential for bacterial growth
-
-
?
2 ATP + 2 L-glutamate + 2 NH3
2 ADP + 2 phosphate + D-glutamine + D-isoglutamine
GlnA2 catalyses the synthesis of D-glutamine and D-isoglutamine
-
-
?
2 ATP + 2 L-glutamate + 2 NH3
2 ADP + 2 phosphate + D-glutamine + D-isoglutamine
GlnA2 catalyses the synthesis of D-glutamine and D-isoglutamine and is essential for bacterial growth
-
-
?
2 ATP + 2 L-glutamate + 2 NH3
2 ADP + 2 phosphate + D-glutamine + D-isoglutamine
GlnA2 catalyses the synthesis of D-glutamine and D-isoglutamine
-
-
?
ADP + L-glutamine + hydroxylamine
gamma-glutamylhydroxamate + ?
-
-
-
r
ADP + L-glutamine + hydroxylamine
gamma-glutamylhydroxamate + ?
-
-
-
r
ADP + phosphate + L-glutamine
ATP + L-glutamate + NH3
-
-
-
r
ADP + phosphate + L-glutamine
ATP + L-glutamate + NH3
-
-
-
r
ATP + 3-aminopentanedioate + hydroxylamine
ADP + phosphate + ?
the enzyme is more selective for L-glutamate (alpha-glutamate) than for 3-aminopentanedioate (beta-glutamate) as a substrate
-
-
?
ATP + 3-aminopentanedioate + hydroxylamine
ADP + phosphate + ?
the enzyme is more selective for L-glutamate (alpha-glutamate) than for 3-aminopentanedioate (beta-glutamate) as a substrate
-
-
?
ATP + 3-aminopentanedioate + hydroxylamine
ADP + phosphate + ?
-
the activity with is 3-aminopentanedioate (beta-glutamate) is 7fold less than the rate obtained with alpha-glutamate
-
-
?
ATP + adipate + NH4+
ADP + phosphate + ?
75% of the activity observed with glutamate
-
-
?
ATP + adipate + NH4+
ADP + phosphate + ?
75% of the activity observed with glutamate
-
-
?
ATP + gamma-aminobutyrate + NH4+
ADP + phosphate + ?
50% of the activity observed with glutamate
-
-
?
ATP + gamma-aminobutyrate + NH4+
ADP + phosphate + ?
50% of the activity observed with glutamate
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
-
-
-
-
r
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
-
central enzyme of nitrogen metabolism
-
-
r
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
-
-
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
-
central enzyme of nitrogen metabolism, ammonia assimilation
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
-
-
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
-
central enzyme of nitrogen metabolism, ammonia assimilation
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
-
-
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
-
central enzyme of nitrogen metabolism, elimination of glutamate from animal brain
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
-
-
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
-
central enzyme of nitrogen metabolism
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
-
central enzyme of nitrogen metabolism, ammonia assimilation
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
-
-
-
-
r
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
-
central enzyme of nitrogen metabolism
-
-
r
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
-
-
-
-
r
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
-
central enzyme of nitrogen metabolism
-
-
r
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
-
-
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
-
central enzyme of nitrogen metabolism, assimilation of ammonia for protein synthesis
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
-
-
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
-
-
-
-
r
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
-
central enzyme of nitrogen metabolism
-
-
r
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
-
central enzyme of nitrogen metabolism, elimination of glutamate from animal brain
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
-
-
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
-
central enzyme of nitrogen metabolism
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
-
-
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
-
central enzyme of nitrogen metabolism
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
-
-
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
-
central enzyme of nitrogen metabolism, elimination of glutamate from animal brain
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
-
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
-
-
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
central enzyme of nitrogen metabolism, postulated to be necessary for the synthesis of the cell wall component poly(L-glutamine-L-glutamate)
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
-
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
central enzyme of nitrogen metabolism, postulated to be necessary for the synthesis of the cell wall component poly(L-glutamine-L-glutamate)
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
-
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
-
-
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
-
central enzyme of nitrogen metabolism, ammonia assimilation
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
-
-
-
-
r
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
-
central enzyme of nitrogen metabolism, ammonia assimilation
-
-
r
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
-
central enzyme of nitrogen metabolism, assimilation of ammonia
-
-
r
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
-
-
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
-
central enzyme of nitrogen metabolism, key enzyme of glutamate metabolism, reduction of local concentrations of glutamate and ammonia
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
-
-
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
-
central enzyme of nitrogen metabolism
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
-
-
-
r
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
central enzyme of nitrogen metabolism
-
-
r
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
-
-
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
-
central enzyme of nitrogen metabolism
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
-
-
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
-
central enzyme of nitrogen metabolism
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
-
-
-
r
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
central enzyme of nitrogen metabolism
-
-
r
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
-
-
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
-
central enzyme of nitrogen metabolism, provides glutamine for biosynthesis, ammonia assimilation
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
-
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
central enzyme of nitrogen metabolism, involved in nitrogen assimilation pathway
-
-
?
ATP + L-Glu + ethylamine
ADP + phosphate + ?
-
slightly effective
-
-
?
ATP + L-Glu + ethylamine
ADP + phosphate + ?
-
slightly effective
-
-
?
ATP + L-Glu + ethylamine
ADP + phosphate + ?
-
slightly effective
-
-
?
ATP + L-Glu + ethylamine
ADP + phosphate + ?
-
slightly effective
-
-
?
ATP + L-Glu + ethylamine
ADP + phosphate + ?
-
slightly effective
-
-
?
ATP + L-Glu + ethylamine
ADP + phosphate + ?
-
slightly effective
-
-
?
ATP + L-Glu + ethylamine
ADP + phosphate + L-Gln + ?
-
1% of the activity with NH4+, at pH 8.0, activated with 30 mM Mg2+
-
-
?
ATP + L-Glu + ethylamine
ADP + phosphate + L-Gln + ?
-
1% of the activity with NH4+, at pH 8.0, activated with 30 mM Mg2+
-
-
?
ATP + L-Glu + hydroxylamine
ADP + phosphate + gamma-glutamyl hydroxamate
-
59% of the activity relative to NH4+
-
-
?
ATP + L-Glu + hydroxylamine
ADP + phosphate + gamma-glutamyl hydroxamate
-
59% of the activity relative to NH4+
-
-
?
ATP + L-Glu + hydroxylamine
ADP + phosphate + gamma-glutamyl hydroxamate
-
13% of the activity relative to NH4+
-
-
?
ATP + L-Glu + hydroxylamine
ADP + phosphate + gamma-glutamyl hydroxamate
-
13% of the activity relative to NH4+
-
-
?
ATP + L-Glu + hydroxylamine
ADP + phosphate + gamma-glutamyl hydroxamate
-
10% of the activity relative to NH4+
-
-
?
ATP + L-Glu + hydroxylamine
ADP + phosphate + gamma-glutamyl hydroxamate
-
10% of the activity relative to NH4+
-
-
?
ATP + L-Glu + hydroxylamine
ADP + phosphate + gamma-glutamyl hydroxamate
-
-
-
?
ATP + L-Glu + hydroxylamine
ADP + phosphate + gamma-glutamyl hydroxamate
-
-
-
?
ATP + L-Glu + hydroxylamine
ADP + phosphate + gamma-glutamyl hydroxamate
-
-
-
-
?
ATP + L-Glu + hydroxylamine
ADP + phosphate + L-Gln + ?
-
32% of the activity with NH4+
-
-
?
ATP + L-Glu + hydroxylamine
ADP + phosphate + L-Gln + ?
-
32% of the activity with NH4+
-
-
?
ATP + L-Glu + methylamine
ADP + phosphate + ?
-
slightly effective
-
-
?
ATP + L-Glu + methylamine
ADP + phosphate + ?
-
slightly effective
-
-
?
ATP + L-Glu + methylamine
ADP + phosphate + ?
-
slightly effective
-
-
?
ATP + L-Glu + methylamine
ADP + phosphate + ?
-
slightly effective
-
-
?
ATP + L-Glu + methylamine
ADP + phosphate + ?
-
slightly effective
-
-
?
ATP + L-Glu + methylamine
ADP + phosphate + ?
-
slightly effective
-
-
?
ATP + L-Glu + NH4+
?
-
glutamate synthetase cycle provides the only efficient pathway for the conversion of inorganic nitrogen to the organic form
-
-
?
ATP + L-Glu + NH4+
?
-
kinetic regulation of this enzyme may play a significant role in ammonia detoxication and rate of formation of Gln-derived neurotransmitters in fish brain
-
-
?
ATP + L-Glu + NH4+
?
-
glutamine produced by the enzyme serves as a source of nitrogen atoms in the biosynthesis of all amino acids, purine and pyrimidine nucleotides, of glucosamine 6-phosphate, 4-aminobenzoic acid, and of nicotinamide derivatives. Glutamine synthetase links the assimilation of NH4+ with biosynthetic pathways leading to the formation of proteins, nucleic acids, complex polysaccharides, and different coenzymes
-
-
?
ATP + L-Glu + NH4+
?
-
roles of the enzyme in pathogenesis of Mycobacterium tuberculosis infection: 1. synthesis of Glu, that is a major component of the cell wall of pathogenic mycobacteria, 2. modulation of the NH4+ level in the Mycobacterium tuberculosis phagosome
-
-
?
ATP + L-Glu + NH4+
?
-
first step at which nitrogen is brought into cellular metabolism, the product Glu, a source of nitrogen in the biosynthesis of many other metabolites
-
-
?
ATP + L-Glu + NH4+
?
-
first step in urea synthesis
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
-
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
-
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
-
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
-
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
-
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
-
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
-
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
-
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
-
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
-
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
-
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
-
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
-
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
-
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
-
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
-
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
-
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
-
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
-
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
-
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
-
-
-
-
ir
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
-
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
-
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
-
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
-
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
-
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
-
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
-
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
-
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
-
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
-
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
-
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
-
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
-
-
37490, 37497, 37511, 37513, 37515, 37529, 37534, 37537, 37541, 37542, 37543, 37563, 660811, 667442 -
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
-
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
-
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
-
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
-
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
-
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
-
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
-
-
-
-
ir
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
-
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
-
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
-
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
-
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
-
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
-
isoenzyme GS1b (EC 6.3.1.2) in concert with NADH-dependent GOGAT (EC 1.4.1.14) constitute the major route of assimilation of ammonium derived from reserve mobilization and glutamic acid/glutamine synthesis in germinating Medicago truncatula seeds. However, during post-germinative growth, although germination is held in darkness, expression of GS2 and Fd-GOGAT (EC 1.4.7.1) increases and expression of GS1b decreases in cotyledons but not in the embryo axis
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
-
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
-
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
-
-
-
-
ir
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
-
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
-
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
-
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
-
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
-
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
-
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
serves for assimilation of ammonium in rice root, and ameliorates the toxic effect of ammonium excess
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
-
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
-
enzyme can bind 8 M of ATP per mol of enzyme
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
-
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
-
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
-
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
-
-
-
ir
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
-
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
-
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
-
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
-
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
-
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
-
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
-
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
-
-
-
-
ir
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
-
1 mol of enzyme can bind 5 M ATP
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
-
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
-
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
-
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
-
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
-
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
-
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
-
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
-
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
-
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
-
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
-
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
-
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
-
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
-
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
-
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
-
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
-
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
-
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
-
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
-
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
-
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
-
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
-
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
-
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
-
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
-
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
-
enzyme form EII is almost absolutely specific for ATP, but enzyme form E1 can also use ITP, GTP and UTP
-
-
?
ATP + L-glutamate + hydroxylamine
?
-
-
-
?
ATP + L-glutamate + hydroxylamine
?
-
-
-
?
ATP + L-glutamate + hydroxylamine
ADP + phosphate + gamma-glutamyl hydroxamate
-
-
-
-
?
ATP + L-glutamate + hydroxylamine
ADP + phosphate + gamma-glutamyl hydroxamate
-
-
-
-
?
ATP + L-glutamate + hydroxylamine
ADP + phosphate + gamma-L-glutamylhydroxamate
the enzyme is more selective for L-glutamate (alpha-glutamate) than for 3-aminopentanedioate (beta-glutamate) as a substrate
-
-
?
ATP + L-glutamate + hydroxylamine
ADP + phosphate + gamma-L-glutamylhydroxamate
the enzyme is more selective for L-glutamate (alpha-glutamate) than for 3-aminopentanedioate (beta-glutamate) as a substrate
-
-
?
ATP + L-glutamate + hydroxylamine
ADP + phosphate + gamma-L-glutamylhydroxamate
the enzyme is more selective for L-glutamate (alpha-glutamate) than for 3-aminopentanedioate (beta-glutamate) as a substrate
-
-
?
ATP + L-glutamate + hydroxylamine
ADP + phosphate + gamma-L-glutamylhydroxamate
-
the activity with L-glutamate is 7fold higher than the rate obtained with 3-aminopentanedioate (beta-glutamate)
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
senescence-specific downregulation of plastidic glutamine synthetase, this is retarded by fertilisation of plants with nitrate or ammonium, but not urea, at the onset of leaf senescence, overview
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
r
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
the enzyme is involved in the regulation of the nitrogen metabolism, overview
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
the enzyme is involved in the signal transduction for regulation of the nitrogen metabolism, overview
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
a two-step reaction with phosphorylation of L-glutamate by ATP to give gamma-glutamyl phosphate followed by addition of ammonia and release of phosphate resulting in L-glutamine, phosphate and ADP
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
a two-step reaction with phosphorylation of L-glutamate by ATP to give gamma-glutamyl phosphate followed by addition of ammonia and release of phosphate resulting in L-glutamine, phosphate and ADP
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
a two-step reaction with phosphorylation of L-glutamate by ATP to give gamma-glutamyl phosphate followed by addition of ammonia and release of phosphate resulting in L-glutamine, phosphate and ADP
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
NH3 in form of NH4Cl
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
dogs show altered L-glutamate distribution and reduced enzyme content in primary glaucoma and ischemia, overview
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
the enzyme activity eliminates cytotoxic ammonia, at the same time converting neurotoxic glutamate to harmless glutamine, enzyme activity defects are linked to neurodegenerative disorders, such as Alzheimer's disease, overview
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
loop movements near the active site generate more closed forms of the eukaryotic enzyme when substrates are bound
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
a two-step reaction with phosphorylation of L-glutamate by ATP to give gamma-glutamyl phosphate followed by addition of ammonia and release of phosphate resulting in L-glutamine, phosphate and ADP
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
a two-step reaction with phosphorylation of L-glutamate by ATP to give gamma-glutamyl phosphate followed by addition of ammonia and release of phosphate resulting in L-glutamine, phosphate and ADP
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
the enzyme is involved in the regulation of nitrogen metabolism and nitrogen fixation via the incorporation of ammonia the glutamine synthetase/glutamate synthase, GS/GOGAT, pathway, overview
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
GlnA1 is essential for survival in vitro, while GlnA2 is probably not
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
the enzyme expressed in the plancenta is actively involved in the provision of glutamine to the fetus
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
a two-step reaction with phosphorylation of L-glutamate by ATP to give gamma-glutamyl phosphate followed by addition of ammonia and release of phosphate resulting in L-glutamine, phosphate and ADP
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
r
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
r
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
isozyme GS2 is involved in osmoregulation of the cells and is part of the chloride regulon of Halobacillus halophilus, overview. At moderate salinities Halobacillus halophilus mainly accumulates glutamine and glutamate to adjust turgor, while it produces proline at high salinity. Halobacillus halophilus also shifts its osmolyte strategy at the transition from the exponential to the stationary phase where proline is exchanged by ectoine, regulation mechanism, overview
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
-
r
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
extracellular glutamate, loss of the glutamate-metabolizing enzyme glutamine synthetase and proliferation of astrocytes are associated with mesial temporal lobe epilepsy, MTLE. Glial proliferation, i.e. gliosis, contributes to the epileptogenicity of the human hippocampus in MTLE, levels of extracellular glutamate are more than five-fold increased in the MTLE hippocampus, glutamate-glutamine cycle, overview
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
glutamine also acts as a signaling molecule, physiological functions of glutamine, overview
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
glutamine synthetase is essential for proliferation of fetal skin fibroblasts
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
the enzyme activity eliminates cytotoxic ammonia, at the same time converting neurotoxic glutamate to harmless glutamine, enzyme activity defects are linked to neurodegenerative disorders, such as Alzheimer's disease, overview
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
a two-step reaction with phosphorylation of L-glutamate by ATP to give gamma-glutamyl phosphate followed by addition of ammonia and release of phosphate resulting in L-glutamine, phosphate and ADP
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
loop movements near the active site generate more closed forms of the eukaryotic enzyme when substrates are bound
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
senescence-specific downregulation of plastidic glutamine synthetase isozyme GS2, this is retarded by fertilisation of plants with nitrate or ammonium, but not urea, at the onset of leaf senescence, GS2 downregulation preceeds upregulation of lysine-ketoglutarate reductase and saccharopine dehydrogenase, overview
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
a two-step reaction with phosphorylation of L-glutamate by ATP to give gamma-glutamyl phosphate followed by addition of ammonia and release of phosphate resulting in L-glutamine, phopshate and ADP
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
r
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
r
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
the enzyme plays a pivotal role in the mammalian brain where it allows neurotransmitter glutamate recycling within astroglia
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
a two-step reaction with phosphorylation of L-glutamate by ATP to give gamma-glutamyl phosphate followed by addition of ammonia and release of phosphate resulting in L-glutamine, phosphate and ADP
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
r
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
GlnA1 catalyses the synthesis of L-glutamine and is nonessential for bacterial growth
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
glnA1 is essential for Mycobacterium tuberculosis virulence
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
GlnA3 catalyses the synthesis of L-glutamine and are nonessential for bacterial growth
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
GlnA4 catalyses the synthesis of L-glutamine and are nonessential for bacterial growth
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
only GlnA1 appears to be the functional enzyme involved in nitrogen metabolism in vivo in the organism, the enzyme is involved in the regulation of nitrogen metabolism and nitrogen fixation via the incorporation of ammonia the glutamine synthetase/glutamate synthase, GS/GOGAT, pathway, overview. GlnA1 is associated with virulence and pathogenicity in Mycobacterium tuberculosis
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
a two-step reaction with phosphorylation of L-glutamate by ATP to give gamma-glutamyl phosphate followed by addition of ammonia and release of phosphate resulting in L-glutamine, phopshate and ADP
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
amino acid binding site and structure, overview
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
GlnA1 catalyses the synthesis of L-glutamine
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
GlnA3 catalyses the synthesis of L-glutamine
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
GlnA4 catalyses the synthesis of L-glutamine
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
r
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
only GlnA1 appears to be the functional enzyme involved in nitrogen metabolism in vivo in the organism, the enzyme is involved in the regulation of nitrogen metabolism and nitrogen fixation via the incorporation of ammonia the glutamine synthetase/glutamate synthase, GS/GOGAT, pathway, overview. GlnA1 is associated with virulence and pathogenicity in Mycobacterium tuberculosis
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
a two-step reaction with phosphorylation of L-glutamate by ATP to give gamma-glutamyl phosphate followed by addition of ammonia and release of phosphate resulting in L-glutamine, phopshate and ADP
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
GlnA1 catalyses the synthesis of L-glutamine and is nonessential for bacterial growth
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
GlnA1 catalyses the synthesis of L-glutamine
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
glnA1 is essential for Mycobacterium tuberculosis virulence
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
amino acid binding site and structure, overview
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
a two-step reaction with phosphorylation of L-glutamate by ATP to give gamma-glutamyl phosphate followed by addition of ammonia and release of phosphate resulting in L-glutamine, phosphate and ADP
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
a two-step reaction with phosphorylation of L-glutamate by ATP to give gamma-glutamyl phosphate followed by addition of ammonia and release of phosphate resulting in L-glutamine, phosphate and ADP
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
the enzyme is involved in regulation of ammonium assimilation requirements during tree development, regulatory mechanism for the transcriptional control of the spatial distribution of cytosolic GS isoforms in pine, overview
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
a two-step reaction with phosphorylation of L-glutamate by ATP to give gamma-glutamyl phosphate followed by addition of ammonia and release of phosphate resulting in L-glutamine, phopshate and ADP
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
GSIII-1, and GSIII-2, no activity of GSI
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
GSIII-1, and GSIII-2, no activity of GSI
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
brain injuries are usually associated with an increase in the expression of the glutamate-converting enzyme glutamine synthetase
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
enzyme regulation involving L-glutamate uptake, Ca2+, and P2X7 receptors, overview
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
the astrocyte-specific glutamine synthetase plays a key role in glutamate recycling and gamma-aminobutyric acid metabolism, it is involved in nitrosative stress response in the brain, overview
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
the enzyme is involved in development of mesial temporal lobe epilepsy, MTLE
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
upon tissue damage, the enzyme endogenous GS is released from glial cells in the extracellular space, where it converts glutamate into glutamine, which is a nonneurotoxic amino acid
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
a two-step reaction with phosphorylation of L-glutamate by ATP to give gamma-glutamyl phosphate followed by addition of ammonia and release of phosphate resulting in L-glutamine, phopshate and ADP
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
a two-step reaction with phosphorylation of L-glutamate by ATP to give gamma-glutamyl phosphate followed by addition of ammonia and release of phosphate resulting in L-glutamine, phosphate and ADP
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
a two-step reaction with phosphorylation of L-glutamate by ATP to give gamma-glutamyl phosphate followed by addition of ammonia and release of phosphate resulting in L-glutamine, phosphate and ADP
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
Sorghum sp.
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
Sorghum sp.
-
a two-step reaction with phosphorylation of L-glutamate by ATP to give gamma-glutamyl phosphate followed by addition of ammonia and release of phosphate resulting in L-glutamine, phosphate and ADP
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
a two-step reaction with phosphorylation of L-glutamate by ATP to give gamma-glutamyl phosphate followed by addition of ammonia and release of phosphate resulting in L-glutamine, phopshate and ADP
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
only GlnA1 appears to be the functional enzyme involved in nitrogen metabolism in vivo in the organism, the enzyme is involved in the regulation of nitrogen metabolism and nitrogen fixation via the incorporation of ammonia the glutamine synthetase/glutamate synthase, GS/GOGAT, pathway, the transcriptional regulator GlnR is involved in regulation of the enzyme activity and is able to function as both an activator and repressor of transcription, overview. GSII probably plays and important role in mycelial development as well as differential glnA1 and glnII transcriptional regulation
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
glutamine synthetase catalyzes the ATP-dependent conversion of ammonia and glutamate to glutamine in the pericentral zone
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
a two-step reaction with phosphorylation of L-glutamate by ATP to give gamma-glutamyl phosphate followed by addition of ammonia and release of phosphate resulting in L-glutamine, phosphate and ADP
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
GS sub-families vary during leaf development and senescence, overview
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
GS sub-families vary during leaf development and senescence, overview. The cytosolic isozymes GS1 and GSr, dominant enzyme forms during leaf senescence, play major roles in assimilating ammonia during the critical phases of remobilisation of nitrogen to the grain, overview
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
a two-step reaction with phosphorylation of L-glutamate by ATP to give gamma-glutamyl phosphate followed by addition of ammonia and release of phosphate resulting in L-glutamine, phosphate and ADP
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
a two-step reaction with phosphorylation of L-glutamate by ATP to give gamma-glutamyl phosphate followed by addition of ammonia and release of phosphate resulting in L-glutamine, phosphate and ADP
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
a two-step reaction with phosphorylation of L-glutamate by ATP to give gamma-glutamyl phosphate followed by addition of ammonia and release of phosphate resulting in L-glutamine, phosphate and ADP
-
-
?
ATP + L-glutamate + NH4+
ADP + phosphate + L-glutamine
-
-
-
-
?
ATP + L-glutamate + NH4+
ADP + phosphate + L-glutamine
glutamine synthetase is a key enzyme in nitrogen assimilation
-
-
?
ATP + L-glutamate + NH4+
ADP + phosphate + L-glutamine
glutamine synthetase is a key enzyme in nitrogen assimilation. Isoenzyme GLN1,1 accumulates in the surface layers of root during nitrogen limitation
-
-
?
ATP + L-glutamate + NH4+
ADP + phosphate + L-glutamine
-
the GLN2 gene product functions in both leaf mitochondria and chloroplasts to faciliate ammonium recovery during photorespiration
-
-
?
ATP + L-glutamate + NH4+
ADP + phosphate + L-glutamine
-
-
-
-
r
ATP + L-glutamate + NH4+
ADP + phosphate + L-glutamine
-
central enzyme of nitrogen metabolism
-
-
r
ATP + L-glutamate + NH4+
ADP + phosphate + L-glutamine
-
-
-
-
r
ATP + L-glutamate + NH4+
ADP + phosphate + L-glutamine
-
central enzyme of nitrogen metabolism
-
-
r
ATP + L-glutamate + NH4+
ADP + phosphate + L-glutamine
-
-
-
-
?
ATP + L-glutamate + NH4+
ADP + phosphate + L-glutamine
-
-
-
?
ATP + L-glutamate + NH4+
ADP + phosphate + L-glutamine
-
-
-
?
ATP + L-glutamate + NH4+
ADP + phosphate + L-glutamine
-
ammonium assimilation by glutamine synthetase is coupled to the function of the ammonium channel AmtB
-
-
?
ATP + L-glutamate + NH4+
ADP + phosphate + L-glutamine
-
it is proposed that the induction of glutamine synthetase genes early in development and the subsequent formation of the active protein are preparatory for the increased capacity of the embryo to convert the toxic nitrogen end product, ammonia, into glutamine, which may then be utilized in the ornithine-urea cycle or other pathways
-
-
?
ATP + L-glutamate + NH4+
ADP + phosphate + L-glutamine
-
-
-
?
ATP + L-glutamate + NH4+
ADP + phosphate + L-glutamine
serves for assimilation of ammonium in rice root, and ameliorates the toxic effect of ammonium excess
-
-
?
ATP + L-glutamate + NH4+
ADP + phosphate + L-glutamine
biosynthesis of glutamine
-
-
?
ATP + L-glutamate + NH4+
ADP + phosphate + L-glutamine
biosynthesis of glutamine
-
-
?
ATP + L-glutamate + NH4+
ADP + phosphate + L-glutamine
the enzyme is specific for glutamate. Aspartate, asparagine or histidine support less than 10% of the activity observed with glutamate. All the other amino acids do not promote ATP hydrolysis
-
-
?
ATP + L-glutamate + NH4+
ADP + phosphate + L-glutamine
the enzyme is specific for glutamate. Aspartate, asparagine or histidine support less than 10% of the activity observed with glutamate. All the other amino acids do not promote ATP hydrolysis
-
-
?
ATP + pentanedioate + NH4+
ADP + phosphate + ?
50% of the activity observed with glutamate
-
-
?
ATP + pentanedioate + NH4+
ADP + phosphate + ?
50% of the activity observed with glutamate
-
-
?
Gln + hydroxylamine + ADP
gamma-Glutamylhydroxamate + NH4+ + ?
-
-
-
-
?
Gln + hydroxylamine + ADP
gamma-Glutamylhydroxamate + NH4+ + ?
-
-
-
?
Gln + hydroxylamine + ADP
gamma-Glutamylhydroxamate + NH4+ + ?
-
-
-
?
Gln + hydroxylamine + ADP
gamma-Glutamylhydroxamate + NH4+ + ?
-
-
-
?
Gln + hydroxylamine + ADP
gamma-Glutamylhydroxamate + NH4+ + ?
-
-
-
?
Gln + hydroxylamine + ADP
gamma-Glutamylhydroxamate + NH4+ + ?
-
-
-
?
Gln + hydroxylamine + ADP
gamma-Glutamylhydroxamate + NH4+ + ?
-
-
-
?
Gln + hydroxylamine + ADP
gamma-Glutamylhydroxamate + NH4+ + ?
-
-
-
-
?
Gln + hydroxylamine + ADP
gamma-Glutamylhydroxamate + NH4+ + ?
-
-
-
?
Gln + hydroxylamine + ADP
gamma-Glutamylhydroxamate + NH4+ + ?
-
maximal transferase activity with ADP, and good activity with AMP and GDP
-
-
?
Gln + hydroxylamine + ADP
gamma-Glutamylhydroxamate + NH4+ + ?
-
maximal transferase activity with ADP, and good activity with AMP and GDP
-
-
?
Gln + hydroxylamine + ADP
gamma-Glutamylhydroxamate + NH4+ + ?
-
-
-
?
Gln + hydroxylamine + ADP
gamma-Glutamylhydroxamate + NH4+ + ?
-
-
-
?
Gln + hydroxylamine + ADP
gamma-Glutamylhydroxamate + NH4+ + ?
-
-
-
?
Gln + hydroxylamine + ADP
gamma-Glutamylhydroxamate + NH4+ + ?
-
-
-
-
?
Gln + hydroxylamine + ADP
gamma-Glutamylhydroxamate + NH4+ + ?
-
ADP or ATP required
-
?
Gln + hydroxylamine + ADP
gamma-Glutamylhydroxamate + NH4+ + ?
-
-
-
-
?
Gln + hydroxylamine + ADP
gamma-Glutamylhydroxamate + NH4+ + ?
-
-
-
-
?
Gln + hydroxylamine + ADP
gamma-Glutamylhydroxamate + NH4+ + ?
-
-
-
?
Gln + hydroxylamine + ADP
gamma-Glutamylhydroxamate + NH4+ + ?
-
-
-
-
?
Gln + hydroxylamine + ADP
gamma-Glutamylhydroxamate + NH4+ + ?
-
-
-
?
Gln + hydroxylamine + ADP
gamma-Glutamylhydroxamate + NH4+ + ?
-
-
-
-
?
Gln + hydroxylamine + ADP
gamma-Glutamylhydroxamate + NH4+ + ?
-
-
-
-
?
Gln + hydroxylamine + ADP
gamma-Glutamylhydroxamate + NH4+ + ?
-
-
-
?
Gln + hydroxylamine + ADP
gamma-Glutamylhydroxamate + NH4+ + ?
-
-
-
-
?
GTP + L-Glu + NH4+
GDP + phosphate + L-Gln
-
15% of the activity relative to ATP
-
-
?
GTP + L-Glu + NH4+
GDP + phosphate + L-Gln
-
15% of the activity relative to ATP
-
-
?
GTP + L-Glu + NH4+
GDP + phosphate + L-Gln
-
no activity
-
-
?
GTP + L-Glu + NH4+
GDP + phosphate + L-Gln
-
no activity
-
-
?
GTP + L-Glu + NH4+
GDP + phosphate + L-Gln
-
no activity
-
-
?
GTP + L-Glu + NH4+
GDP + phosphate + L-Gln
-
no activity
-
-
?
GTP + L-Glu + NH4+
GDP + phosphate + L-Gln
-
59% of the activity relative to ATP
-
-
?
GTP + L-Glu + NH4+
GDP + phosphate + L-Gln
-
45% of the activity relative to ATP
-
-
?
GTP + L-Glu + NH4+
GDP + phosphate + L-Gln
-
26% of the activity with ATP
-
-
?
GTP + L-Glu + NH4+
GDP + phosphate + L-Gln
-
26% of the activity with ATP
-
-
?
GTP + L-Glu + NH4+
GDP + phosphate + L-Gln
-
enzyme form EII is almost absolutely specific for ATP, but enzyme form E1 can also use ITP, GTP and UTP
-
-
?
hydroxylamine + L-glutamine + ATP
L-gamma-glutamyl-hydroxamate + ammonia + ADP
gamma-glutamylhydroxamate synthetase activity
-
-
?
hydroxylamine + L-glutamine + ATP
L-gamma-glutamyl-hydroxamate + ammonia + ADP
gamma-glutamylhydroxamate synthetase activity
-
-
?
hydroxylamine + L-glutamine + ATP
L-gamma-glutamyl-hydroxamate + ammonia + ADP
-
gamma-glutamylhydroxamate synthetase activity, GSI, GSIII-1, and GSIII-2
-
-
r
hydroxylamine + L-glutamine + ATP
L-gamma-glutamyl-hydroxamate + ammonia + ADP
-
gamma-glutamylhydroxamate synthetase activity, GSI, GSIII-1, and GSIII-2
-
-
r
hydroxylamine + L-glutamine + ATP
L-gamma-glutamyl-hydroxamate + ammonium + ADP
gamma-glutamylhydroxamate synthetase activity
-
-
r
hydroxylamine + L-glutamine + ATP
L-gamma-glutamyl-hydroxamate + ammonium + ADP
gamma-glutamylhydroxamate synthetase activity
-
-
r
ITP + L-Glu + NH4+
IDP + phosphate + L-Gln
-
32% of the activity relative to ATP
-
-
?
ITP + L-Glu + NH4+
IDP + phosphate + L-Gln
-
18% of the activity with ATP
-
-
?
ITP + L-Glu + NH4+
IDP + phosphate + L-Gln
-
18% of the activity with ATP
-
-
?
ITP + L-Glu + NH4+
IDP + phosphate + L-Gln
-
enzyme form EII is almost absolutely specific for ATP, but E1 can also use ITP, GTP and UTP
-
-
?
L-Gln + hydroxylamine + ADP
gamma-glutamylhydroxamate + NH4+ + ?
-
-
-
-
?
L-Gln + hydroxylamine + ADP
gamma-glutamylhydroxamate + NH4+ + ?
-
-
-
-
?
L-glutamine + hydroxylamine + ADP
gamma-glutamylhydroxamate + NH4+ + ?
-
-
-
-
?
L-glutamine + hydroxylamine + ADP
gamma-glutamylhydroxamate + NH4+ + ?
gamma-glutamyltransferase activity
-
-
?
L-glutamine + hydroxylamine + ADP
gamma-glutamylhydroxamate + NH4+ + ?
gamma-glutamyltransferase activity
-
-
?
UTP + L-Glu + NH4+
UDP + phosphate + L-Gln
-
10% of the activity relative to ATP
-
-
?
UTP + L-Glu + NH4+
UDP + phosphate + L-Gln
-
enzyme form EII is almost absolutely specific for ATP, but E1 can also use ITP, GTP and UTP
-
-
?
additional information
?
-
-
feedback-inhibited glutamine synthetase acts as a molecular chaperone to stabilize the association of dimers of transcripion factor GlnR, the repressor of the glutamine synthetase operon in Bacillus subtilis, with their DNA binding sites, molecular mechanism, overview. The cell shuts off synthesis of GS, and hence of glutamine, when both the enzyme and its product are in excess. The feedback-inhibited enzyme also regulates the activity of TnrA, the global regulator of nitrogen metabolism genes, but by a very different mechanism, overview
-
-
?
additional information
?
-
-
the glutamine synthetase transmits the nitrogen regulatory signal to GlnR, a transcription factor involved in nitrogen metabolism regulation, the enzyme interacts with GlnR via the factor's C-terminal autoinhibitory domain, the protein-protein interaction of GlnR and glutamine synthetase stabilizes the GlnR-DNA complexes, interaction analysis of enzyme with wild-type and truncated GlnR proteins, overview
-
-
?
additional information
?
-
structure-activity relationship, overview
-
-
?
additional information
?
-
-
the feedback-inhibited enzyme, acting as a chaperone, is required for the binding of transcription factor GlnR to DNA, the feedback inhibition of GS by L-glutamine induces the sequence-specific binding of transcription factor GlnR to DNA in nitrogen metabolism regulation by 32fold and reduces the dissociation rate by 18fold stabilizing the complexes, overview
-
-
?
additional information
?
-
-
structure-activity relationship, overview
-
-
?
additional information
?
-
-
structure-activity relationship, overview
-
-
?
additional information
?
-
the role of GS in humans depends on tissue localization. In the brain, it regulates the levels of toxic ammonia and converts neurotoxic glutamate to harmless glutamine, whereas in the liver, it is one of the enzymes responsible for the removal of ammonia
-
-
?
additional information
?
-
-
the role of GS in humans depends on tissue localization. In the brain, it regulates the levels of toxic ammonia and converts neurotoxic glutamate to harmless glutamine, whereas in the liver, it is one of the enzymes responsible for the removal of ammonia
-
-
?
additional information
?
-
active site structure analysis, conformational changes near the active sites upon ligand binding, overview
-
-
?
additional information
?
-
-
active site structure analysis, conformational changes near the active sites upon ligand binding, overview
-
-
?
additional information
?
-
-
structure-activity relationship, overview
-
-
?
additional information
?
-
-
structure-activity relationship, overview
-
-
?
additional information
?
-
-
the enzyme acts as an acetyl-CoA independent acetyltransferase mediating the transfer of acetyl group(s) from polyphenolic acetates to certain functional proteins in mammalian cells, e.g. protein acetylation by a model acetoxy drug 7, 8-diacetoxy-4-methylcoumarin, or acetylation and inhibition of glutathione transferase using polyphenolic actetate, overview
-
-
?
additional information
?
-
-
structure-activity relationship, overview
-
-
?
additional information
?
-
GS is involved in the assimilation of ammonia in the plant. GS catalyzes the ATP-dependent condensation of NH3 with glutamate to produce glutamine
-
-
?
additional information
?
-
-
GS is involved in the assimilation of ammonia in the plant. GS catalyzes the ATP-dependent condensation of NH3 with glutamate to produce glutamine
-
-
?
additional information
?
-
regulation of ammonium assimilation in Haloferax mediterranei involves complex formation between glutamine synthetase and two GlnK proteins, overview. The protein-protein interaction increases glutamine synthetase activity in the presence of 2-oxoglutarate
-
-
?
additional information
?
-
regulation of ammonium assimilation in Haloferax mediterranei involves complex formation between glutamine synthetase and two GlnK proteins, overview. The protein-protein interaction increases glutamine synthetase activity in the presence of 2-oxoglutarate
-
-
?
additional information
?
-
-
regulation of ammonium assimilation in Haloferax mediterranei involves complex formation between glutamine synthetase and two GlnK proteins, overview. The protein-protein interaction increases glutamine synthetase activity in the presence of 2-oxoglutarate
-
-
?
additional information
?
-
-
elevations in c-jun may be a potential cause of the glutamine synthetase deficiency in mesial temporal lobe epilepsy, MTLE, pathology, overview. The enzyme is also regulated by glucocorticoids and proinflammatory cytokines
-
-
?
additional information
?
-
-
extracellular glutamate in the hippocampus causes recurrent seizures and is involved in medically intractable mesial temporal lobe epilepsy, MTLE, overview
-
-
?
additional information
?
-
-
loss of glutamine synthetase activity either inherited or induced through L-methionine sulfoximine leads to an upregulation of the glutamine synthetase protein but not of the glutamine synthetase mRNA and results in a significant drop in the proliferation rate but has no effect on apoptosis. Exogenous glutamine does not influence the rate of apoptosis but increases proliferation rates of the fetal but not the mature fibroblasts
-
-
?
additional information
?
-
the enzyme is a target for activation through the signal transducer protein Wnt in the Wnt pathway, overview
-
-
?
additional information
?
-
-
the role of GS in humans depends on tissue localization. In the brain, it regulates the levels of toxic ammonia and converts neurotoxic glutamate to harmless glutamine, whereas in the liver, one of the enzymes is responsible for the removal of ammonia
-
-
?
additional information
?
-
-
under healthy conditions, the major site of glutamine utilization is the absorptive columnar epithelium of the small intestine, where glutamine serves as the major respiratory fuel of enterocytes, interorgan flux of glutamine, overview
-
-
?
additional information
?
-
-
Wnt and steroid pathways control glutamate signalling by regulating glutamine synthetase activity in osteoblastic cells, overview
-
-
?
additional information
?
-
-
active site structure analysis, conformational changes near the active sites upon ligand binding, overview
-
-
?
additional information
?
-
structure-activity relationship, overview
-
-
?
additional information
?
-
-
structure-activity relationship, overview
-
-
?
additional information
?
-
structure-activity relationship, overview
-
-
?
additional information
?
-
structure-activity relationship, overview
-
-
?
additional information
?
-
-
essential enzyme involved in the pathogenicity of Mycobacterium tuberculosis
-
-
?
additional information
?
-
glutamine synthetase is involved in nitrogen metabolism, and four enzymes are regulating glutamine synthetase activity and/or nitrogen and glutamate metabolism: adenylyl transferase, i.e. GlnE, gamma-glutamylcysteine synthase, i.e. GshA, UDP-N-acetylmuramoylalanine-D-glutamate ligase, i.e. MurD, and glutamate racemase, i.e. MurI
-
-
?
additional information
?
-
glutamine synthetase is involved in nitrogen metabolism, and four enzymes are regulating glutamine synthetase activity and/or nitrogen and glutamate metabolism: adenylyl transferase, i.e. GlnE, gamma-glutamylcysteine synthase, i.e. GshA, UDP-N-acetylmuramoylalanine-D-glutamate ligase, i.e. MurD, and glutamate racemase, i.e. MurI
-
-
?
additional information
?
-
glutamine synthetase is involved in nitrogen metabolism, and four enzymes are regulating glutamine synthetase activity and/or nitrogen and glutamate metabolism: adenylyl transferase, i.e. GlnE, gamma-glutamylcysteine synthase, i.e. GshA, UDP-N-acetylmuramoylalanine-D-glutamate ligase, i.e. MurD, and glutamate racemase, i.e. MurI
-
-
?
additional information
?
-
-
glutamine synthetase is involved in nitrogen metabolism, and four enzymes are regulating glutamine synthetase activity and/or nitrogen and glutamate metabolism: adenylyl transferase, i.e. GlnE, gamma-glutamylcysteine synthase, i.e. GshA, UDP-N-acetylmuramoylalanine-D-glutamate ligase, i.e. MurD, and glutamate racemase, i.e. MurI
-
-
?
additional information
?
-
structure-activity relationship, overview
-
-
?
additional information
?
-
structure-activity relationship, overview
-
-
?
additional information
?
-
glutamine synthetase is involved in nitrogen metabolism, and four enzymes are regulating glutamine synthetase activity and/or nitrogen and glutamate metabolism: adenylyl transferase, i.e. GlnE, gamma-glutamylcysteine synthase, i.e. GshA, UDP-N-acetylmuramoylalanine-D-glutamate ligase, i.e. MurD, and glutamate racemase, i.e. MurI
-
-
?
additional information
?
-
-
the enzyme acts as an acetyl-CoA independent acetyltransferase mediating the transfer of acetyl group(s) from polyphenolic acetates to certain functional proteins in mammalian cells, e.g. protein acetylation by a model acetoxy drug 7, 8-diacetoxy-4-methylcoumarin, or acetylation and inhibition of glutathione transferase using polyphenolic actetate, substrate specificity, overview. The TAase activity of MTAase is independent of the catalytic activity of the glutamine synthetase
-
-
?
additional information
?
-
-
the enzyme acts as an acetyl-CoA independent acetyltransferase mediating the transfer of acetyl group(s) from polyphenolic acetates to certain functional proteins in mammalian cells, e.g. protein acetylation by a model acetoxy drug 7, 8-diacetoxy-4-methylcoumarin, or acetylation and inhibition of glutathione transferase using polyphenolic actetate, substrate specificity, overview. The TAase activity of MTAase is independent of the catalytic activity of the glutamine synthetase
-
-
?
additional information
?
-
-
structure-activity relationship, overview
-
-
?
additional information
?
-
-
structure-activity relationship, overview
-
-
?
additional information
?
-
PpDof5 has an antagonistic regulatory function in the expression of GS1a and GS1b promoters in pine protoplasts transfected with the transcription factor under control of CaMV 35S promoter, overview
-
-
?
additional information
?
-
-
PpDof5 has an antagonistic regulatory function in the expression of GS1a and GS1b promoters in pine protoplasts transfected with the transcription factor under control of CaMV 35S promoter, overview
-
-
?
additional information
?
-
-
structure-activity relationship, overview
-
-
?
additional information
?
-
-
the isozymes show glutamine gamma-transferase activity, overview. Activities of the isozymes catalyzing ATP hydrolysis, overview. GSI has an about 100fold lower ATPase activity compared to ATPase activities of GSIII-1 and -2
-
-
?
additional information
?
-
-
the isozymes show glutamine gamma-transferase activity, overview. Activities of the isozymes catalyzing ATP hydrolysis, overview. GSI has an about 100fold lower ATPase activity compared to ATPase activities of GSIII-1 and -2
-
-
?
additional information
?
-
-
glutamine synthetase is likely to play a regulatory role in the control of sporulation
-
-
?
additional information
?
-
in reactions in which Mn2+ is used, GTP, UTP, and CTP havea limited ability to replace ATP (less than 30%), while in reactions in which Mg2+ was used, complete inhibition by these NTPs is observed. Broad NTP specificity of hyperthermophilic archaeon synthetases suggests that enzymes of ancestral life forms can utilize various NTPs besides ATP
-
-
?
additional information
?
-
-
in reactions in which Mn2+ is used, GTP, UTP, and CTP havea limited ability to replace ATP (less than 30%), while in reactions in which Mg2+ was used, complete inhibition by these NTPs is observed. Broad NTP specificity of hyperthermophilic archaeon synthetases suggests that enzymes of ancestral life forms can utilize various NTPs besides ATP
-
-
?
additional information
?
-
in reactions in which Mn2+ is used, GTP, UTP, and CTP havea limited ability to replace ATP (less than 30%), while in reactions in which Mg2+ was used, complete inhibition by these NTPs is observed. Broad NTP specificity of hyperthermophilic archaeon synthetases suggests that enzymes of ancestral life forms can utilize various NTPs besides ATP
-
-
?
additional information
?
-
-
deficiency in hippocampal glutamine synthetase causes recurrent seizures, even in the absence of classical mesial temporal sclerosis, overview
-
-
?
additional information
?
-
-
glutamine synthetase protects the spinal cord against hypoxia-induced and GABA(A) receptor-activated axonal depressions, it may inhibit the depression of CAP amplitudes by blocking GABAA receptors, overview. GS significantly reduces the axonal depression effects of isoguvacine
-
-
?
additional information
?
-
-
rats with pentylenetetrazole-induced repetitive epileptic seizures show increased heat shock responseand reduced enzyme activity, overview
-
-
?
additional information
?
-
structure-activity relationship, overview
-
-
?
additional information
?
-
structure-activity relationship, overview
-
-
?
additional information
?
-
-
structure-activity relationship, overview
-
-
?
additional information
?
-
Sorghum sp.
-
structure-activity relationship, overview
-
-
?
additional information
?
-
-
structure-activity relationship, overview
-
-
?
additional information
?
-
-
enzyme form GS2 shows maximal activity under photoautotrophic conditions, enzyme form GS1 shows maximal activity under heterotrophic conditions
-
-
?
additional information
?
-
transcriptional regulation as part of the nitrogen assimilation system, overview
-
-
?
additional information
?
-
-
transcriptional regulation as part of the nitrogen assimilation system, overview
-
-
?
additional information
?
-
structure-activity relationship, overview
-
-
?
additional information
?
-
-
structure-activity relationship, overview
-
-
?
additional information
?
-
-
structure-activity relationship, overview
-
-
?
additional information
?
-
-
structure-activity relationship, overview
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2 ATP + 2 L-glutamate + 2 NH3
2 ADP + 2 phosphate + D-glutamine + D-isoglutamine
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
ATP + L-glutamate + NH4+
ADP + phosphate + L-glutamine
additional information
?
-
2 ATP + 2 L-glutamate + 2 NH3
2 ADP + 2 phosphate + D-glutamine + D-isoglutamine
GlnA2 catalyses the synthesis of D-glutamine and D-isoglutamine and is essential for bacterial growth
-
-
?
2 ATP + 2 L-glutamate + 2 NH3
2 ADP + 2 phosphate + D-glutamine + D-isoglutamine
GlnA2 catalyses the synthesis of D-glutamine and D-isoglutamine and is essential for bacterial growth
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
-
central enzyme of nitrogen metabolism
-
-
r
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
-
central enzyme of nitrogen metabolism, ammonia assimilation
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
-
central enzyme of nitrogen metabolism, ammonia assimilation
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
-
central enzyme of nitrogen metabolism, elimination of glutamate from animal brain
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
-
central enzyme of nitrogen metabolism
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
-
central enzyme of nitrogen metabolism, ammonia assimilation
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
-
central enzyme of nitrogen metabolism
-
-
r
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
-
central enzyme of nitrogen metabolism
-
-
r
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
-
central enzyme of nitrogen metabolism, assimilation of ammonia for protein synthesis
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
-
central enzyme of nitrogen metabolism
-
-
r
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
-
central enzyme of nitrogen metabolism, elimination of glutamate from animal brain
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
-
central enzyme of nitrogen metabolism
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
-
central enzyme of nitrogen metabolism
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
-
central enzyme of nitrogen metabolism, elimination of glutamate from animal brain
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
central enzyme of nitrogen metabolism, postulated to be necessary for the synthesis of the cell wall component poly(L-glutamine-L-glutamate)
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
central enzyme of nitrogen metabolism, postulated to be necessary for the synthesis of the cell wall component poly(L-glutamine-L-glutamate)
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
-
central enzyme of nitrogen metabolism, ammonia assimilation
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
-
central enzyme of nitrogen metabolism, ammonia assimilation
-
-
r
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
-
central enzyme of nitrogen metabolism, assimilation of ammonia
-
-
r
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
-
central enzyme of nitrogen metabolism, key enzyme of glutamate metabolism, reduction of local concentrations of glutamate and ammonia
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
-
central enzyme of nitrogen metabolism
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
central enzyme of nitrogen metabolism
-
-
r
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
-
central enzyme of nitrogen metabolism
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
-
central enzyme of nitrogen metabolism
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
central enzyme of nitrogen metabolism
-
-
r
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
-
central enzyme of nitrogen metabolism, provides glutamine for biosynthesis, ammonia assimilation
-
-
?
ATP + glutamate + NH4+
ADP + phosphate + L-glutamine
central enzyme of nitrogen metabolism, involved in nitrogen assimilation pathway
-
-
?
ATP + L-Glu + NH4+
?
-
glutamate synthetase cycle provides the only efficient pathway for the conversion of inorganic nitrogen to the organic form
-
-
?
ATP + L-Glu + NH4+
?
-
kinetic regulation of this enzyme may play a significant role in ammonia detoxication and rate of formation of Gln-derived neurotransmitters in fish brain
-
-
?
ATP + L-Glu + NH4+
?
-
glutamine produced by the enzyme serves as a source of nitrogen atoms in the biosynthesis of all amino acids, purine and pyrimidine nucleotides, of glucosamine 6-phosphate, 4-aminobenzoic acid, and of nicotinamide derivatives. Glutamine synthetase links the assimilation of NH4+ with biosynthetic pathways leading to the formation of proteins, nucleic acids, complex polysaccharides, and different coenzymes
-
-
?
ATP + L-Glu + NH4+
?
-
roles of the enzyme in pathogenesis of Mycobacterium tuberculosis infection: 1. synthesis of Glu, that is a major component of the cell wall of pathogenic mycobacteria, 2. modulation of the NH4+ level in the Mycobacterium tuberculosis phagosome
-
-
?
ATP + L-Glu + NH4+
?
-
first step at which nitrogen is brought into cellular metabolism, the product Glu, a source of nitrogen in the biosynthesis of many other metabolites
-
-
?
ATP + L-Glu + NH4+
?
-
first step in urea synthesis
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
-
-
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
-
isoenzyme GS1b (EC 6.3.1.2) in concert with NADH-dependent GOGAT (EC 1.4.1.14) constitute the major route of assimilation of ammonium derived from reserve mobilization and glutamic acid/glutamine synthesis in germinating Medicago truncatula seeds. However, during post-germinative growth, although germination is held in darkness, expression of GS2 and Fd-GOGAT (EC 1.4.7.1) increases and expression of GS1b decreases in cotyledons but not in the embryo axis
-
-
?
ATP + L-Glu + NH4+
ADP + phosphate + L-Gln
serves for assimilation of ammonium in rice root, and ameliorates the toxic effect of ammonium excess
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
senescence-specific downregulation of plastidic glutamine synthetase, this is retarded by fertilisation of plants with nitrate or ammonium, but not urea, at the onset of leaf senescence, overview
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
r
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
the enzyme is involved in the regulation of the nitrogen metabolism, overview
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
the enzyme is involved in the signal transduction for regulation of the nitrogen metabolism, overview
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
dogs show altered L-glutamate distribution and reduced enzyme content in primary glaucoma and ischemia, overview
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
the enzyme activity eliminates cytotoxic ammonia, at the same time converting neurotoxic glutamate to harmless glutamine, enzyme activity defects are linked to neurodegenerative disorders, such as Alzheimer's disease, overview
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
the enzyme is involved in the regulation of nitrogen metabolism and nitrogen fixation via the incorporation of ammonia the glutamine synthetase/glutamate synthase, GS/GOGAT, pathway, overview
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
the enzyme expressed in the plancenta is actively involved in the provision of glutamine to the fetus
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
r
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
r
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
isozyme GS2 is involved in osmoregulation of the cells and is part of the chloride regulon of Halobacillus halophilus, overview. At moderate salinities Halobacillus halophilus mainly accumulates glutamine and glutamate to adjust turgor, while it produces proline at high salinity. Halobacillus halophilus also shifts its osmolyte strategy at the transition from the exponential to the stationary phase where proline is exchanged by ectoine, regulation mechanism, overview
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
-
r
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
extracellular glutamate, loss of the glutamate-metabolizing enzyme glutamine synthetase and proliferation of astrocytes are associated with mesial temporal lobe epilepsy, MTLE. Glial proliferation, i.e. gliosis, contributes to the epileptogenicity of the human hippocampus in MTLE, levels of extracellular glutamate are more than five-fold increased in the MTLE hippocampus, glutamate-glutamine cycle, overview
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
glutamine also acts as a signaling molecule, physiological functions of glutamine, overview
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
glutamine synthetase is essential for proliferation of fetal skin fibroblasts
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
the enzyme activity eliminates cytotoxic ammonia, at the same time converting neurotoxic glutamate to harmless glutamine, enzyme activity defects are linked to neurodegenerative disorders, such as Alzheimer's disease, overview
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
senescence-specific downregulation of plastidic glutamine synthetase isozyme GS2, this is retarded by fertilisation of plants with nitrate or ammonium, but not urea, at the onset of leaf senescence, GS2 downregulation preceeds upregulation of lysine-ketoglutarate reductase and saccharopine dehydrogenase, overview
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
r
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
r
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
the enzyme plays a pivotal role in the mammalian brain where it allows neurotransmitter glutamate recycling within astroglia
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
r
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
GlnA1 catalyses the synthesis of L-glutamine and is nonessential for bacterial growth
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
glnA1 is essential for Mycobacterium tuberculosis virulence
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
GlnA3 catalyses the synthesis of L-glutamine and are nonessential for bacterial growth
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
GlnA4 catalyses the synthesis of L-glutamine and are nonessential for bacterial growth
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
only GlnA1 appears to be the functional enzyme involved in nitrogen metabolism in vivo in the organism, the enzyme is involved in the regulation of nitrogen metabolism and nitrogen fixation via the incorporation of ammonia the glutamine synthetase/glutamate synthase, GS/GOGAT, pathway, overview. GlnA1 is associated with virulence and pathogenicity in Mycobacterium tuberculosis
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
r
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
only GlnA1 appears to be the functional enzyme involved in nitrogen metabolism in vivo in the organism, the enzyme is involved in the regulation of nitrogen metabolism and nitrogen fixation via the incorporation of ammonia the glutamine synthetase/glutamate synthase, GS/GOGAT, pathway, overview. GlnA1 is associated with virulence and pathogenicity in Mycobacterium tuberculosis
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
GlnA1 catalyses the synthesis of L-glutamine and is nonessential for bacterial growth
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
glnA1 is essential for Mycobacterium tuberculosis virulence
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
the enzyme is involved in regulation of ammonium assimilation requirements during tree development, regulatory mechanism for the transcriptional control of the spatial distribution of cytosolic GS isoforms in pine, overview
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
brain injuries are usually associated with an increase in the expression of the glutamate-converting enzyme glutamine synthetase
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
enzyme regulation involving L-glutamate uptake, Ca2+, and P2X7 receptors, overview
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
the astrocyte-specific glutamine synthetase plays a key role in glutamate recycling and gamma-aminobutyric acid metabolism, it is involved in nitrosative stress response in the brain, overview
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
the enzyme is involved in development of mesial temporal lobe epilepsy, MTLE
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
upon tissue damage, the enzyme endogenous GS is released from glial cells in the extracellular space, where it converts glutamate into glutamine, which is a nonneurotoxic amino acid
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
Sorghum sp.
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
only GlnA1 appears to be the functional enzyme involved in nitrogen metabolism in vivo in the organism, the enzyme is involved in the regulation of nitrogen metabolism and nitrogen fixation via the incorporation of ammonia the glutamine synthetase/glutamate synthase, GS/GOGAT, pathway, the transcriptional regulator GlnR is involved in regulation of the enzyme activity and is able to function as both an activator and repressor of transcription, overview. GSII probably plays and important role in mycelial development as well as differential glnA1 and glnII transcriptional regulation
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
glutamine synthetase catalyzes the ATP-dependent conversion of ammonia and glutamate to glutamine in the pericentral zone
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
GS sub-families vary during leaf development and senescence, overview
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
GS sub-families vary during leaf development and senescence, overview. The cytosolic isozymes GS1 and GSr, dominant enzyme forms during leaf senescence, play major roles in assimilating ammonia during the critical phases of remobilisation of nitrogen to the grain, overview
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
?
ATP + L-glutamate + NH3
ADP + phosphate + L-glutamine
-
-
-
-
?
ATP + L-glutamate + NH4+
ADP + phosphate + L-glutamine
glutamine synthetase is a key enzyme in nitrogen assimilation
-
-
?
ATP + L-glutamate + NH4+
ADP + phosphate + L-glutamine
glutamine synthetase is a key enzyme in nitrogen assimilation. Isoenzyme GLN1,1 accumulates in the surface layers of root during nitrogen limitation
-
-
?
ATP + L-glutamate + NH4+
ADP + phosphate + L-glutamine
-
the GLN2 gene product functions in both leaf mitochondria and chloroplasts to faciliate ammonium recovery during photorespiration
-
-
?
ATP + L-glutamate + NH4+
ADP + phosphate + L-glutamine
-
central enzyme of nitrogen metabolism
-
-
r
ATP + L-glutamate + NH4+
ADP + phosphate + L-glutamine
-
central enzyme of nitrogen metabolism
-
-
r
ATP + L-glutamate + NH4+
ADP + phosphate + L-glutamine
-
ammonium assimilation by glutamine synthetase is coupled to the function of the ammonium channel AmtB
-
-
?
ATP + L-glutamate + NH4+
ADP + phosphate + L-glutamine
-
it is proposed that the induction of glutamine synthetase genes early in development and the subsequent formation of the active protein are preparatory for the increased capacity of the embryo to convert the toxic nitrogen end product, ammonia, into glutamine, which may then be utilized in the ornithine-urea cycle or other pathways
-
-
?
ATP + L-glutamate + NH4+
ADP + phosphate + L-glutamine
serves for assimilation of ammonium in rice root, and ameliorates the toxic effect of ammonium excess
-
-
?
additional information
?
-
-
feedback-inhibited glutamine synthetase acts as a molecular chaperone to stabilize the association of dimers of transcripion factor GlnR, the repressor of the glutamine synthetase operon in Bacillus subtilis, with their DNA binding sites, molecular mechanism, overview. The cell shuts off synthesis of GS, and hence of glutamine, when both the enzyme and its product are in excess. The feedback-inhibited enzyme also regulates the activity of TnrA, the global regulator of nitrogen metabolism genes, but by a very different mechanism, overview
-
-
?
additional information
?
-
-
the glutamine synthetase transmits the nitrogen regulatory signal to GlnR, a transcription factor involved in nitrogen metabolism regulation, the enzyme interacts with GlnR via the factor's C-terminal autoinhibitory domain, the protein-protein interaction of GlnR and glutamine synthetase stabilizes the GlnR-DNA complexes, interaction analysis of enzyme with wild-type and truncated GlnR proteins, overview
-
-
?
additional information
?
-
the role of GS in humans depends on tissue localization. In the brain, it regulates the levels of toxic ammonia and converts neurotoxic glutamate to harmless glutamine, whereas in the liver, it is one of the enzymes responsible for the removal of ammonia
-
-
?
additional information
?
-
-
the role of GS in humans depends on tissue localization. In the brain, it regulates the levels of toxic ammonia and converts neurotoxic glutamate to harmless glutamine, whereas in the liver, it is one of the enzymes responsible for the removal of ammonia
-
-
?
additional information
?
-
-
the enzyme acts as an acetyl-CoA independent acetyltransferase mediating the transfer of acetyl group(s) from polyphenolic acetates to certain functional proteins in mammalian cells, e.g. protein acetylation by a model acetoxy drug 7, 8-diacetoxy-4-methylcoumarin, or acetylation and inhibition of glutathione transferase using polyphenolic actetate, overview
-
-
?
additional information
?
-
GS is involved in the assimilation of ammonia in the plant. GS catalyzes the ATP-dependent condensation of NH3 with glutamate to produce glutamine
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-
?
additional information
?
-
-
GS is involved in the assimilation of ammonia in the plant. GS catalyzes the ATP-dependent condensation of NH3 with glutamate to produce glutamine
-
-
?
additional information
?
-
regulation of ammonium assimilation in Haloferax mediterranei involves complex formation between glutamine synthetase and two GlnK proteins, overview. The protein-protein interaction increases glutamine synthetase activity in the presence of 2-oxoglutarate
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-
?
additional information
?
-
regulation of ammonium assimilation in Haloferax mediterranei involves complex formation between glutamine synthetase and two GlnK proteins, overview. The protein-protein interaction increases glutamine synthetase activity in the presence of 2-oxoglutarate
-
-
?
additional information
?
-
-
regulation of ammonium assimilation in Haloferax mediterranei involves complex formation between glutamine synthetase and two GlnK proteins, overview. The protein-protein interaction increases glutamine synthetase activity in the presence of 2-oxoglutarate
-
-
?
additional information
?
-
-
elevations in c-jun may be a potential cause of the glutamine synthetase deficiency in mesial temporal lobe epilepsy, MTLE, pathology, overview. The enzyme is also regulated by glucocorticoids and proinflammatory cytokines
-
-
?
additional information
?
-
-
extracellular glutamate in the hippocampus causes recurrent seizures and is involved in medically intractable mesial temporal lobe epilepsy, MTLE, overview
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-
?
additional information
?
-
-
loss of glutamine synthetase activity either inherited or induced through L-methionine sulfoximine leads to an upregulation of the glutamine synthetase protein but not of the glutamine synthetase mRNA and results in a significant drop in the proliferation rate but has no effect on apoptosis. Exogenous glutamine does not influence the rate of apoptosis but increases proliferation rates of the fetal but not the mature fibroblasts
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-
?
additional information
?
-
the enzyme is a target for activation through the signal transducer protein Wnt in the Wnt pathway, overview
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-
?
additional information
?
-
-
the role of GS in humans depends on tissue localization. In the brain, it regulates the levels of toxic ammonia and converts neurotoxic glutamate to harmless glutamine, whereas in the liver, one of the enzymes is responsible for the removal of ammonia
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-
?
additional information
?
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-
under healthy conditions, the major site of glutamine utilization is the absorptive columnar epithelium of the small intestine, where glutamine serves as the major respiratory fuel of enterocytes, interorgan flux of glutamine, overview
-
-
?
additional information
?
-
-
Wnt and steroid pathways control glutamate signalling by regulating glutamine synthetase activity in osteoblastic cells, overview
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-
?
additional information
?
-
-
essential enzyme involved in the pathogenicity of Mycobacterium tuberculosis
-
-
?
additional information
?
-
glutamine synthetase is involved in nitrogen metabolism, and four enzymes are regulating glutamine synthetase activity and/or nitrogen and glutamate metabolism: adenylyl transferase, i.e. GlnE, gamma-glutamylcysteine synthase, i.e. GshA, UDP-N-acetylmuramoylalanine-D-glutamate ligase, i.e. MurD, and glutamate racemase, i.e. MurI
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-
?
additional information
?
-
glutamine synthetase is involved in nitrogen metabolism, and four enzymes are regulating glutamine synthetase activity and/or nitrogen and glutamate metabolism: adenylyl transferase, i.e. GlnE, gamma-glutamylcysteine synthase, i.e. GshA, UDP-N-acetylmuramoylalanine-D-glutamate ligase, i.e. MurD, and glutamate racemase, i.e. MurI
-
-
?
additional information
?
-
glutamine synthetase is involved in nitrogen metabolism, and four enzymes are regulating glutamine synthetase activity and/or nitrogen and glutamate metabolism: adenylyl transferase, i.e. GlnE, gamma-glutamylcysteine synthase, i.e. GshA, UDP-N-acetylmuramoylalanine-D-glutamate ligase, i.e. MurD, and glutamate racemase, i.e. MurI
-
-
?
additional information
?
-
-
glutamine synthetase is involved in nitrogen metabolism, and four enzymes are regulating glutamine synthetase activity and/or nitrogen and glutamate metabolism: adenylyl transferase, i.e. GlnE, gamma-glutamylcysteine synthase, i.e. GshA, UDP-N-acetylmuramoylalanine-D-glutamate ligase, i.e. MurD, and glutamate racemase, i.e. MurI
-
-
?
additional information
?
-
glutamine synthetase is involved in nitrogen metabolism, and four enzymes are regulating glutamine synthetase activity and/or nitrogen and glutamate metabolism: adenylyl transferase, i.e. GlnE, gamma-glutamylcysteine synthase, i.e. GshA, UDP-N-acetylmuramoylalanine-D-glutamate ligase, i.e. MurD, and glutamate racemase, i.e. MurI
-
-
?
additional information
?
-
-
the enzyme acts as an acetyl-CoA independent acetyltransferase mediating the transfer of acetyl group(s) from polyphenolic acetates to certain functional proteins in mammalian cells, e.g. protein acetylation by a model acetoxy drug 7, 8-diacetoxy-4-methylcoumarin, or acetylation and inhibition of glutathione transferase using polyphenolic actetate, substrate specificity, overview. The TAase activity of MTAase is independent of the catalytic activity of the glutamine synthetase
-
-
?
additional information
?
-
-
the enzyme acts as an acetyl-CoA independent acetyltransferase mediating the transfer of acetyl group(s) from polyphenolic acetates to certain functional proteins in mammalian cells, e.g. protein acetylation by a model acetoxy drug 7, 8-diacetoxy-4-methylcoumarin, or acetylation and inhibition of glutathione transferase using polyphenolic actetate, substrate specificity, overview. The TAase activity of MTAase is independent of the catalytic activity of the glutamine synthetase
-
-
?
additional information
?
-
PpDof5 has an antagonistic regulatory function in the expression of GS1a and GS1b promoters in pine protoplasts transfected with the transcription factor under control of CaMV 35S promoter, overview
-
-
?
additional information
?
-
-
PpDof5 has an antagonistic regulatory function in the expression of GS1a and GS1b promoters in pine protoplasts transfected with the transcription factor under control of CaMV 35S promoter, overview
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-
?
additional information
?
-
-
glutamine synthetase is likely to play a regulatory role in the control of sporulation
-
-
?
additional information
?
-
-
deficiency in hippocampal glutamine synthetase causes recurrent seizures, even in the absence of classical mesial temporal sclerosis, overview
-
-
?
additional information
?
-
-
glutamine synthetase protects the spinal cord against hypoxia-induced and GABA(A) receptor-activated axonal depressions, it may inhibit the depression of CAP amplitudes by blocking GABAA receptors, overview. GS significantly reduces the axonal depression effects of isoguvacine
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-
?
additional information
?
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-
rats with pentylenetetrazole-induced repetitive epileptic seizures show increased heat shock responseand reduced enzyme activity, overview
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?
additional information
?
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enzyme form GS2 shows maximal activity under photoautotrophic conditions, enzyme form GS1 shows maximal activity under heterotrophic conditions
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?
additional information
?
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transcriptional regulation as part of the nitrogen assimilation system, overview
-
-
?
additional information
?
-
-
transcriptional regulation as part of the nitrogen assimilation system, overview
-
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?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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2-oxoglutarate
directly stimulates activity
Al3+
results in 8.91tivity compared to Mg2+
Ba2+
increases the activity of wild-type and mutant enzymes at 1 mM
Fe3+
increases the activity of wild-type and mutant enzymes at 1 mM
NH4+
increases the activity of the mutant enzymes at 1 mM
Ca2+
results in 43.9% activity compared to Mg2+
Ca2+
-
stimulates activity at 1 mM
Ca2+
can partially substitute for Mg2+
Ca2+
can substitute for Mg2+ in biosynthesis of glutamine with 30% of the efficiency obtained with Mg2+
Cd2+
-
0.5 mM, activity rises by 96%
Cd2+
-
activates enzyme form EII more than EI
Cl-
-
increases the affinity of the enzyme 2fold to 4fold for Mg2+ or Mn2+
Cl-
chloride stimulates the production of active enzyme by about 300%, in the absence of chloride in the assay buffer, glutamine synthetase activity is decreased by as much as 90%
Cl-
Cl- dependence of glutamine synthetase activity
Cl-
the enzyme's expression partially and activity strictly depends on chloride, strongly salinity-dependent expression of gene glnA2 with a maximal increase of transcripts of about 4fold at 1.5 M NaCl or higher compared to the value at 0.4 M NaCl, expression of glnA1 is not influenced by different salinities, optimal enzyme activity at 2.5 M NaCl or higher, chloride dependent regulatory network, overview
Co2+
results in 109.1% activity compared to Mg2+
Co2+
-
required, strongly bound to enzyme, can not be removed by dialysis, removal of metal ions with EDTA results in conformational changes
Co2+
-
strongly increases activity in combination with Mg2+
Co2+
-
supports the enzymatic activity
Co2+
-
maximal activity when Co2+ is in excess of ATP
Co2+
-
divalent cation required, Mn2+, Co2+, or Mg2+. Mn2+ is most effective
Co2+
-
maximal activity at a ration of ATP to Co2+ of 1.0. The addition of 3 mM Co2+ to the biosynthetic reaction mixtures containing 4 mM Mg2+ results in a 3-7-fold increase in activity
Co2+
-
divalent cation required, Mn2+, Co2+, or Mg2+. Mn2+ is most effective
Co2+
-
maximal activity at a ration of ATP to Co2+ of 1.0. The addition of 3 mM Co2+ to the biosynthetic reaction mixtures containing 4 mM Mg2+ results in a 3-7-fold increase in activity
Co2+
-
divalent cation required, Mn2+, Co2+, or Mg2+. Mn2+ is most effective
Co2+
-
activates, isoenzyme GS1
Co2+
-
activates, isoenzyme GS2
Co2+
-
can partially replace Mn2+ in transferase reaction
Co2+
increases the activity of the mutant enzymes at 1 mM
Co2+
-
stimulates activity at 1 mM
Co2+
-
divalent cation required, decreasing order of effectiveness at 10 mM in transferase activity: Mn2+, Cu2+, Mg2+, Co2+. For biosynthetic activity: Mg2+, Mn2+, Zn2+/Cu2+, Ni2+
Co2+
-
partially effective as activator of biosynthetic activity and transferase activity, half-maximal activation of biosynthetic reaction at 6.3 mM
Co2+
-
at pH 7.2, Mg2+ is more effective than Co2+
Co2+
-
can partially replace Mg2+ in activation
Co2+
enzyme activity is dependent on the presence of divalent cations. Co2+ is able to support activity levels above 50% compared with magnesium in standard conditions of substrates, temperature and pH
Co2+
-
only enzyme form E1 is activated
Cu2+
results in 22.2% activity compared to Mg2+
Cu2+
-
stimulates activity at 1 mM
Cu2+
-
divalent cation required, decreasing order of effectiveness at 10 mM in transferase activity: Mn2+, Cu2+, Mg2+, Co2+. For biosynthetic activity: Mg2+, Mn2+, Zn2+/Cu2+, Ni2+
Cu2+
-
partially effective as activator of transferase activity
Fe2+
results in 22.3% activity compared to Mg2+
Fe2+
-
stimulates activity at 1 mM
K+
-
strongly stimulates transferase activity
K+
increases the activity of wild-type and mutant enzymes at 1 mM
K+
-
0.25 mM as optimal concentration for highest activity
Li+
-
50 mM LiCl increases activity
Li+
increases the activity of the mutant enzymes at 1 mM
Li+
-
50 mM LiCl increases activity
Li+
-
50 mM LiCl increases activity
Li+
-
50 mM LiCl increases activity
Mg2+
-
Mg2+
assay in presence of 55 mM Mg2+
Mg2+
-
required, most effective, strongly bound to enzyme, can not be removed by dialysis, removal of metal ions with EDTA results in conformational changes
Mg2+
-
required, preferred over Mn2+ at alkaline and neutral pH
Mg2+
-
supports the enzymatic activity
Mg2+
-
divalent cation required, Mn2+, Co2+, or Mg2+. Mn2+ is most effective. Activity is maximal when Mg2+ is in excess of ATP
Mg2+
-
divalent cation required, Mn2+, Co2+, or Mg2+. Mn2+ is most effective. Activity is maximal when Mg2+ is in excess of ATP
Mg2+
-
divalent cation required, Mn2+, Co2+, or Mg2+. Mn2+ is most effective. Activity is maximal when Mg2+ is in excess of ATP
Mg2+
-
the enzyme has one structural site per subunit for Mn2+ or Mg2+ and a second site per subunit for metal ion-nucleotide complex, both of which must be filled for activity expression
Mg2+
the active site of the apoenzyme structure contains only a single Mg2+, rather than Mn2+, ion bound at the n1 position
Mg2+
-
activates, most effectice cation, isoenzyme GS1
Mg2+
-
activates, most effectice cation, isoenzyme GS2
Mg2+
-
can partially replace Mn2+ in transferase reaction
Mg2+
-
maximal activity at a ratio of Mg2+ to ATP of 2
Mg2+
-
divalent cation required, specificity for Mg2+ in the biosynthetic assay
Mg2+
-
maximal activity at 30 mM
Mg2+
binding amino acid residues, overview
Mg2+
-
gamma-glutamyltransferase activity of wild-type, unadenylated enzyme is supported by either Mn2+ or Mg2+, while the adenylated enzyme is active only with Mn2+ in absence of Mg2+. The Y397F mutant behaves as the unadenylated form, consistent with its inability to be adenylated. Mutant enzymes Y397A and Y397S behave as if they are adenylated
Mg2+
required, increases the activity of wild-type and mutant enzymes at 1 mM
Mg2+
-
stimulates activity at 1 mM
Mg2+
the activity increases 225% in the presence of 5 mM Mn2+ compared to 50 mM Mg2+
Mg2+
-
required, less efficient than Mn2+
Mg2+
-
optimal ratio of Mg2+ to ATP is 3:1
Mg2+
assay in presence of 55 mM Mg2+
Mg2+
-
assay in presence of 55 mM Mg2+
Mg2+
-
divalent cation required, specificity for Mg2+ in the biosynthetic assay
Mg2+
required, two ions bound to enzyme
Mg2+
activation up to 25 mM, inhibition above
Mg2+
to be in its active state, the enzyme requires magnesium or manganese ions, located in three metal sites designated as n1-n3
Mg2+
-
divalent cation required, order of effectiveness at 10 mM in transferase activity: Mn2+, Cu2+, Mg2+, Co2+. For biosynthetic activity: Mg2+, Mn2+, Zn2+, Cu2+, Ni2+
Mg2+
-
divalent cation required, specificity for Mg2+ in the biosynthetic assay
Mg2+
-
essential activator for biosynthetic activity, half-maximal activation at 18 mM. Partially effective as activator of transferase activity
Mg2+
-
activates, optimum: 15 mM
Mg2+
-
optimal ratio of MgCl2 to ATP is 2:1 at 1 mM ATP, inhibition at more than 20 mM excess of MgCl2 over ATP
Mg2+
-
at pH 7.2, Mg2+ is more effective than Mn2+
Mg2+
clear preference for Mg2+ in glutamine biosynthesis, optimal concentration is 50 mM
Mg2+
-
divalent metal ion required, Mg2+ is most effective. Maximal activation of GS1 at 5 mM and of GS2 at 20 mM
Mg2+
-
Mg2+ in excess of that required for formation of MgATP2- is required for maximal activity
Mg2+
required for activity and for stability
Mg2+
strong inhibition on the Thermotoga maritima activity in extracts of Escherichia coli cells grown in the presence of ammonia
Mg2+
-
required for optimum activity of enzyme from strain SA0, no activation of enzyme from strain SA1
Mg2+
enzyme activity is dependent on the presence of divalent cations. Mg2+ is the most effective cation
Mg2+
-
required, Mg2+ is an integral component of the enzyme glutamine synthetase having both a structural and a catalytic role. Mg2+ is relevant for the posttranslational regulation of the enzyme
Mg2+
-
divalent cation required, enzyme form EI is more active with Mg2+ than with Mn2+, but EII is more active with Mn2+ than Mg2+
Mn2+
results in 17.12% activity compared to Mg2+
Mn2+
-
required, preferred over Mg2+ at acidic pH
Mn2+
-
slight activation, strongly bound to enzyme, can not be removed by dialysis, removal of metal ions with EDTA results in conformational changes
Mn2+
-
supports the enzymatic activity
Mn2+
required for gamma-glutamylhydroxamate synthetase activity
Mn2+
-
MnCl2 stimulates gamma-glutamyl transferase activity of glutamine synthethase from unshocked cells, no effect on the gamma-glutamyl transferase activity of unshocked cells
Mn2+
-
divalent cation required, Mn2+, Co2+, or Mg2+. Mn2+ is most effective. Activity is maximal at a ratio of ATP to Mn2+ of 1.0
Mn2+
-
divalent cation required, Mn2+, Co2+, or Mg2+. Mn2+ is most effective. Activity is maximal at a ratio of ATP to Mn2+ of 1.0
Mn2+
-
divalent cation required, Mn2+, Co2+, or Mg2+. Mn2+ is most effective. Activity is maximal at a ratio of ATP to Mn2+ of 1.0
Mn2+
-
the enzyme has one structural site per subunit for Mn2+ or Mg2+ and a second site per subunit for metal ion-nucleotide complex, both of which must be filled for activity expression
Mn2+
-
required for transferase activity
Mn2+
-
maximal synthetase activity occurs when the ratio of Mg2+ to ATP is 2
Mn2+
-
maximal activity at 1 mM
Mn2+
-
required for transferase activity
Mn2+
-
gamma-glutamyltransferase activity of wild-type, unadenylated enzyme is supported by either Mn2+ or Mg2+, while the adenylated enzyme is active only with Mn2+ in absence of Mg2+. The Y397F mutant behaves as the unadenylated form, consistent with its inability to be adenylated. Mutant enzymes Y397A and Y397S behave as if they are adenylated
Mn2+
-
most effective cation for stimulation of activity at 1 mM
Mn2+
the activity increases 225% in the presence of 5 mM Mn2+ compared to 50 mM Mg2+
Mn2+
-
required, highest activity at 0.6-1 mM, higher concentrations inhibitory
Mn2+
-
three enzyme-bound Mn2+ ions, an additional Mn2+ ion makes contacts with Glu196 and the inorganic phosphate
Mn2+
can partially substitute for Mg2+
Mn2+
-
supports activity of adenylylated and deadenylylated enzyme, no other divalent cation can support gamma-glutamyl transferase activity, optimal concentration is 0.3 mM
Mn2+
required, two ions bound to enzyme
Mn2+
to be in its active state, the enzyme requires magnesium or manganese ions, located in three metal sites designated as n1-n3
Mn2+
-
divalent cation required, order of effectiveness at 10 mM in transferase activity: Mn2+, Cu2+, Mg2+, Co2+. For biosynthetic activity: Mg2+, Mn2+, Zn2+, Cu2+, Ni2+
Mn2+
-
required for transferase activity
Mn2+
-
required for transferase activity
Mn2+
-
required, optimal concentrations of Mn2+ ions for GSI, GSIII-1, and GSIII-2 activities are 0.25, 0.5, and 1 mM, respectively
Mn2+
-
activates with 11% of the efficiency of the activation with Mg2+, optimum: 3-4 mM
Mn2+
-
at pH 7.2, Mg2+ is more effective than Mn2+
Mn2+
-
optimal concentration is 2 mM, 25% of the maximal activity relative to Mg2+ activation
Mn2+
-
required, optimum concentration around 0.5 mM
Mn2+
-
activity of the low-activity form is higher than that of the high-activity form in the Mn2+-dependent biosynthetic assay
Mn2+
optimal concentration is 1 mM, activates gamma-glutamyltransferase activity, glutamine synthetase type III. Can substitute for Mg2+ in biosynthesis of glutamine with 30% of the efficiency obtained with Mg2+
Mn2+
-
can partially replace Mg2+ in activation
Mn2+
-
cannot effectively replace Mg2+
Mn2+
required for activity and for stability
Mn2+
-
required for optimum activity of enzyme from strain SA1, highest activity at 0.3 mM, concentration inhibitory for enzyme from SA0
Mn2+
enzyme activity is dependent on the presence of divalent cations. Mn2+ is able to support activity levels above 50% compared with magnesium in standard conditions of substrates, temperature and pH
Mn2+
-
essential for activity, contains three Mn2+ ions per subunit
Mn2+
-
divalent cation required, enzyme form EI is more active with Mg2+ than with Mn2+, but EII is more active with Mn2+ than Mg2+
Na+
increases the activity of wild-type and mutant enzymes at 1 mM
Na+
3 mM, highest activity
Na+
-
0.5 mM as optimal concentration for highest activity
Na+
-
highest activity at 50 mM
Ni2+
results in 8.92% activity compared to Mg2+
Ni2+
increases the activity of the mutant enzymes at 1 mM
Ni2+
-
stimulates activity at 1 mM
Ni2+
can partially substitute for Mg2+
Ni2+
-
divalent cation required, decreasing order of effectiveness at 10 mM in transferase activity: Mn2+, Cu2+, Mg2+, Co2+. For biosynthetic activity: Mg2+, Mn2+, Zn2+/Cu2+, Ni2+
Zn2+
results in 9.58% activity compared to Mg2+
Zn2+
increases the activity of the mutant enzymes at 1 mM
Zn2+
-
stimulates activity at 1 mM
Zn2+
can partially substitute for Mg2+
Zn2+
-
divalent cation required, decreasing order of effectiveness at 10 mM in transferase activity: Mn2+, Cu2+, Mg2+, Co2+. For biosynthetic activity: Mg2+, Mn2+, Zn2+/Cu2+, Ni2+
Zn2+
-
partially effective as activator of biosynthetic activity, half-maximal activation at 6.3 mM
additional information
-
Mg2+, Cu2+, Co2+, or Ca2+ cannot substitute for Mn2+
additional information
little or no detectable activity with Mg2+, Ca2+, Co2+ or Fe2+
additional information
-
little or no detectable activity with Mg2+, Ca2+, Co2+ or Fe2+
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(1,4-diamino-4-oxobutyl)phosphonic acid
-
(1-amino-4-methoxy-4-oxobutyl)phosphonic acid
-
(1R,3R)-1-amino-3-(hydroxy(methyl)phosphoryl)cyclohexane-1-carboxylic acid
-
(1R,3R)-1-amino-3-(hydroxy(methyl)phosphoryl)cyclohexanecarboxylic acid
(1R,3R)-1-amino-3-(hydroxy(methyl)phosphoryl)cyclopentane-1-carboxylic acid
-
(1R,3R)-1-amino-3-(hydroxy(methyl)phosphoryl)cyclopentanecarboxylic acid
-
racemic mixture
(2R)-2-amino-4-(hydroxyamino)butanoic acid
-
(2R)-2-amino-4-(S-methane-N-phosphonosulfonimidoyl)butanoic acid
-
(2R)-2-amino-4-(S-methanesulfonimidoyl)butanoic acid
-
(2R,3S)-3-aminooxetane-2-carboxylic acid
(2S)-2-amino-4-(hydroxyamino)butanoic acid
(2S)-2-amino-4-(methylsulfonyl)butanoic acid
-
(2S)-2-amino-4-(S-methanesulfonimidoyl)butanoic acid
-
(2S)-2-amino-4-(S-methyl-N-phosphonosulfonimidoyl)butanoic acid
-
-
(2S)-2-amino-4-(S-methylsulfonimidoyl)butanoic acid
-
-
(2S)-2-amino-4-[(1-aminoethyl)(hydroxy)phosphoryl]butanoic acid
(2S)-2-amino-4-[(2-aminoethyl)(hydroxy)phosphoryl]butanoic acid
-
-
(2S)-2-amino-4-[(3S)-3-hydroxy-2-oxoazetidin-3-yl]butanoic acid
-
irrversible
(2S)-2-amino-4-[(aminomethyl)(hydroxy)phosphoryl]butanoic acid
(2S)-2-amino-4-[hydroxy(hydroxymethyl)phosphoryl]butanoic acid
(2S)-2-amino-4-[hydroxy(nitroso)amino]butanoic acid
-
(2S,5R)-2,6-diamino-5-hydroxyhexanoic acid
docks at the amino acid binding site of the enzyme, structure, overview
(3,4-diamino-4-oxobutyl)methylphosphinic acid
-
(3-amino-4-methoxy-4-oxobutyl)methylphosphinic acid
-
(3-methanesulfinylphenylamino)acetic acid
30% inhibition at 1.0 mM
(5S)-5-hydroxy-D-lysine
-
(NH4)2SO4
-
weak, gamma-glutamyl transferase activity
(R)-3-hydroxy-2-(3-sulfamoylphenylamino)propionic acid
33% inhibition at 1.0 mM
(R)-methionine sulfoximine phosphate
(S)-3-hydroxy-2-(3-methanesulfinylphenylamino)propionic acid
13% inhibition at 1.0 mM
(S)-methionine sulfoximine phosphate
([[(2,4-dichlorophenyl)methyl]amino]methylene)bis(phosphonic acid)
-
([[(2,5-dichlorophenyl)methyl]amino]methylene)bis(phosphonic acid)
-
([[2-(4-hydroxyphenyl)ethyl]amino]methanediyl)bis(phosphonic acid)
-
-
1-[(3,4-dichlorophenyl)methyl]-3,7-dimethyl-8-(morpholin-4-yl)-3,7-dihydro-1H-purine-2,6-dione
-
1-[(3,4-dichlorophenyl)methyl]-3,7-dimethyl-8-morpholin-4-yl-purine-2,6-dione
-
1-[(3,4-dichlorophenyl)methyl]-8-[(2-methoxyethyl)amino]-3,7-dimethyl-3,7-dihydro-1H-purine-2,6-dione
-
2-(3-aminophenyl)-6-bromo-N-cyclopentylimidazo[1,2-a]pyridin-3-amine
-
-
2-amino-2-ethyl-4-(S-methylsulfonimidoyl)butanoic acid
-
41% inhibition at 0.4 mM
2-amino-2-ethyl-4-[hydroxy(methyl)phosphoryl]butanoic acid
2-amino-4-(hydroxyamino)butanoic acid
-
2-amino-4-(methanesulfinyl)butanoic acid
60% inhibition at 10 mM
2-amino-4-(methanesulfonyl)butanoic acid
78% inhibition at 10 mM
2-amino-4-(S-ethylsulfonimidoyl)butanoic acid
-
76.4% inhibition at 10 mM
2-amino-4-(S-propylsulfonimidoyl)butanoic acid
-
35.8% inhibition at 20 mM
2-amino-4-hydroxyglutaric acid
-
-
2-amino-4-phosphonobutanoic acid
-
2-amino-4-sulfamoylbutanoic acid
-
2-amino-4-[(3,4-dichlorobenzyl)(hydroxy)phosphoryl]butanoic acid
-
20% inhibition at 12.5 mM
2-amino-4-[(3,5-dimethylbenzyl)(hydroxy)phosphoryl]butanoic acid
-
20% inhibition at 12.5 mM
2-amino-4-[(4-bromobenzyl)(hydroxy)phosphoryl]butanoic acid
-
20% inhibition at 12.5 mM
2-amino-4-[(aminomethyl)(hydroxy)phosphoryl]butanoic acid
-
2-amino-4-[(carboxymethyl)(hydroxy)phosphoryl]butanoic acid
-
20% inhibition at 12.5 mM
2-amino-4-[(phosphonomethyl)sulfonyl]butanoic acid
2-amino-4-[benzyl(hydroxy)phosphoryl]butanoic acid
-
30% inhibition at 12.5 mM
2-amino-4-[ethyl(hydroxy)phosphoryl]butanoic acid
2-amino-4-[hydroxy(oxido)phosphanyl]butanoic acid
-
35% inhibition at 12.5 mM
2-amino-4-[hydroxy(phenyl)phosphoryl]butanoic acid
-
30% inhibition at 0.5 mM
2-amino-4-[hydroxy(phosphonomethyl)amino]butanoic acid
-
50% inhibition at 0.5 mM
2-amino-4-[hydroxy(phosphonomethyl)phosphoryl]butanoic acid
2-amino-4-[methyl(phosphonomethyl)amino]butanoic acid
-
29% inhibition at 0.5 mM
2-amino-4-[methyl(phosphonomethyl)phosphoryl]butanoic acid
-
-
2-oxo-2,3-dihydro-1H-benzimidazole-5-sulfonamide
24% inhibition at 1.0 mM
2-tert-butyl-4-(6-methoxynaphthalen-2-yl)-5-phenyl-1H-imidazole
-
-
2-[(1H-benzimidazol-1-yl)methoxy]ethyl diethyl phosphate
competitive versus ATP
2-[(diphosphonomethyl)amino]pyridine-3-carboxylic acid
-
-
2-[2-tert-butyl-4-(6-methoxynaphthalen-2-yl)-1H-imidazol-5-yl]pyrimidine
-
-
2-[4-[6-bromo-3-(butylamino)imidazo[1,2-a]pyridin-2-yl]phenoxy]acetamide
-
2-[4-[6-bromo-3-(butylamino)imidazo[1,2-a]pyridin-2-yl]phenoxy]ethan-1-ol
-
2-[[4-[6-bromo-3-(butylamino)imidazo[1,2-a]pyridin-2-yl]phenyl](methyl)amino]ethan-1-ol
-
3,4-dichlorophenylethylidene-1-hydroxy-1,1-bisphosphonic acid
-
3,5-difluorophenylaminoethylidenebisphosphonic acid
-
3-amino-5-[hydroxy(methyl)phosphoryl]tetrahydrofuran-3-carboxylic acid
-
-
3-[(1H-1,2,4-triazol-3-ylcarbonyl)amino]benzoic acid
26% inhibition at 1.0 mM
3-[(diphosphonomethyl)amino]benzoic acid
-
-
3-[(phosphonoacetyl)amino]alanine
3-[2-tert-butyl-5-(pyridin-4-yl)-1H-imidazol-4-yl]quinoline
-
-
3-[4-(6-methoxynaphthalen-2-yl)-5-(pyridin-4-yl)-1H-imidazol-2-yl]phenol
-
-
3-[6-bromo-3-(butylamino)imidazo[1,2-a]pyridin-2-yl]benzoic acid
-
3-[6-bromo-3-(butylamino)imidazo[1,2-a]pyridin-2-yl]phenol
-
3-[6-bromo-3-(cyclopentylamino)imidazo[1,2-a]pyridin-2-yl]benzoic acid
3-[6-bromo-3-(cyclopentylamino)imidazo[1,2-a]pyridin-2-yl]phenol
4-(2-tert-butyl-4-(6-methoxynaphthalen-2-yl)-1H-imidazol-5-yl)pyridin-2-amine
-
-
4-(S-ethylsulfonimidoyl)isovaline
-
25.8% inhibition at 2 mM
4-(S-methylsulfonimidoyl)isovaline
-
80% inhibition at 0.1 mM
4-(S-propylsulfonimidoyl)isovaline
-
34.6% inhibition at 20 mM
4-amino-4-phosphonobutanoic acid
-
4-amino-4-phosphonopentanoic acid
-
4-amino-4-[hydroxy(methyl)phosphoryl]butanoic acid
-
4-amino-4-[hydroxy(methyl)phosphoryl]pentanoic acid
-
4-fluoroglutamic acid
-
-
4-methylphenylethylidene-1-hydroxy-1,1-bisphosphonic acid
-
4-[(oxan-2-yl)oxy]-1-(prop-2-en-1-yl)-1H-pyrazolo[3,4-d]pyrimidine
competitive versus ATP
4-[2-ethyl-4-(6-methoxynaphthalen-2-yl)-1H-imidazol-5-yl]pyridine
-
-
4-[2-tert-butyl-4-(6-methoxynaphthalen-2-yl)-1H-imidazol-5-yl]-2-fluoropyridine
-
-
4-[2-tert-butyl-4-(6-methoxynaphthalen-2-yl)-1H-imidazol-5-yl]-N,N-dimethylpyridin-2-amine
-
-
4-[2-tert-butyl-4-(6-methoxynaphthalen-2-yl)-1H-imidazol-5-yl]-N-methylpyridin-2-amine
-
-
4-[2-tert-butyl-4-(6-methoxynaphthalen-2-yl)-1H-imidazol-5-yl]pyridin-2(1H)-one
-
-
4-[2-tert-butyl-4-(6-methoxynaphthalen-2-yl)-1H-imidazol-5-yl]pyridin-2-amine
4-[2-tert-butyl-4-(6-methoxynaphthalen-2-yl)-1H-imidazol-5-yl]pyridine
4-[4-(6-methoxynaphthalen-2-yl)-1H-imidazol-5-yl]pyridine
-
-
4-[4-(6-methoxynaphthalen-2-yl)-2-(1H-pyrrol-2-yl)-1H-imidazol-5-yl]pyridine
-
-
4-[4-(6-methoxynaphthalen-2-yl)-2-(2-phenylpropan-2-yl)-1H-imidazol-5-yl]pyridine
-
-
4-[4-(6-methoxynaphthalen-2-yl)-2-(phenoxymethyl)-1H-imidazol-5-yl]pyridine
-
-
4-[4-(6-methoxynaphthalen-2-yl)-2-methyl-1H-imidazol-5-yl]pyridine
-
-
4-[4-(6-methoxynaphthalen-2-yl)-2-phenyl-1H-imidazol-5-yl]pyridine
-
-
4-[hydroxy(methyl)phosphoryl]homoserine
-
4-[hydroxy(methyl)phosphoryl]isovaline
4-[hydroxy(methyl)phosphoryl]norvaline
-
5'-p-fluorosulfonylbenzoyladenosine
5-(2-methoxyethyl)-9-phenyl-5,10-dihydro-4H-imidazo[1,2-a]indeno[1,2-e]pyrazin-4-one
-
5-(3-methylbutyl)-9-(pyridin-3-yl)-5,10-dihydro-4H-imidazo[1,2-a]indeno[1,2-e]pyrazin-4-one
-
5-(but-3-en-1-yl)-9-(pyridin-3-yl)-5,10-dihydro-4H-imidazo[1,2-a]indeno[1,2-e]pyrazin-4-one
-
5-benzyl-9-phenyl-5,10-dihydro-4H-imidazo[1,2-a]indeno[1,2-e]pyrazin-4-one
-
5-cyclopropyl-9-(pyridin-2-yl)-5,10-dihydro-4H-imidazo[1,2-a]indeno[1,2-e]pyrazin-4-one
-
5-methyl-9-phenyl-5,10-dihydro-4H-imidazo[1,2-a]indeno[1,2-e]pyrazin-4-one
-
5-oxo-6-phosphononorleucine
5-[(3-amino-3-carboxypropyl)(hydroxy)phosphoryl]norvaline
-
20% inhibition at 12.5 mM
5-[2-tert-butyl-4-(6-methoxynaphthalen-2-yl)-1H-imidazol-5-yl]pyrimidine
-
-
5-[3-(dimethylamino)propyl]-9-(3-methoxyphenyl)-5,10-dihydro-4H-imidazo[1,2-a]indeno[1,2-e]pyrazin-4-one
-
5-[3-(dimethylamino)propyl]-9-(pyridin-2-yl)-5,10-dihydro-4H-imidazo[1,2-a]indeno[1,2-e]pyrazin-4-one
-
5-[3-(dimethylamino)propyl]-9-(pyridin-3-yl)-5,10-dihydro-4H-imidazo[1,2-a]indeno[1,2-e]pyrazin-4-one
-
5-[6-bromo-3-(butylamino)imidazo[1,2-a]pyridin-2-yl]-2-methoxyphenol
-
5-[6-bromo-3-(cyclopentylamino)imidazo[1,2-a]pyridin-2-yl]-2-methoxyphenol
5-[6-iodo-3-(cyclopentylamino)imidazo[1,2-a]pyridin-2-yl]-2-methoxyphenol
-
-
6-bromo-N-butyl-2-[4-[2-(dimethylamino)ethoxy]phenyl]imidazo[1,2-a]pyridin-3-amine
-
8-azidoadenosine
-
in presence of Mg2+ or Mn2+
9-(3-chlorophenyl)-5,10-dihydro-4H-imidazo[1,2-a]indeno[1,2-e]pyrazin-4-one
-
9-(3-methoxyphenyl)-5,10-dihydro-4H-imidazo[1,2-a]indeno[1,2-e]pyrazin-4-one
-
9-(pyridin-3-yl)-5,10-dihydro-4H-imidazo[1,2-a]indeno[1,2-e]pyrazin-4-one
-
9-(quinolin-5-yl)-5,10-dihydro-4H-imidazo[1,2-a]indeno[1,2-e]pyrazin-4-one
-
9-bromo-5,10-dihydro-4H-imidazo[1,2-a]indeno[1,2-e]pyrazin-4-one
-
9-phenyl-5,10-dihydro-4H-imidazo[1,2-a]indeno[1,2-e]pyrazin-4-one
-
9-phenyl-5-(prop-2-en-1-yl)-5,10-dihydro-4H-imidazo[1,2-a]indeno[1,2-e]pyrazin-4-one
-
alanine
-
more inhibitory for enzyme from strain SA0 than for enzyme from SA1
ascorbate
-
little loss of activity with 2 mM ascorbate alone. Complete inactivation by co-incubation with 1 mM H2O2, 0.002 mM Fe3+, 2 mM ascorbate for 30 min
aspartate
-
more inhibitory for enzyme from strain SA0 than for enzyme from SA1
benzylethylidene-1-hydroxy-1,1-bisphosphonic acid
-
Beta amyloid peptides
-
-
-
Carbamoyl-phosphoalanine
-
-
Cd2+
-
0.5 mM, activity is reduced by 60%
diethyl [2-(3-hydroxyanilino)-2-oxoethyl]phosphonate
competitive versus ATP
dithioerythritol
-
no inhibition of wild type enzyme, inhibits activity of D56A and D56E mutant enzymes
DMSO
about 15% activation at 2%
Fe3+
-
no loss of activity with 0.002 mM Fe3+ alone. Complete inactivation by co-incubation with 1 mM H2O2, 0.002 mM Fe3+, 2 mM ascorbate for 30 min
glucosamine 6-phosphate
-
-
iodoacetamide
inhibits isozyme MtGS1a
ITP
-
biosynthetic reaction
L-arginine
-
inhibitory at high concentrations
L-glutamate
-
in the presence of Mn2+ the activity decreases when exceeding a concentration of 10 mM glutamate
L-glutamyl gamma-phosphinic acid
L-Glycine
-
decreases the enzyme activity considerably
L-methionine S-sulfoximine
-
IC50: 3 mM
L-methionine-(S)-sulfoximine
docks at the amino acid binding site of the enzyme, structure, overview
L-methionine-(S,R)-sulfoximine
-
L-methionine-(S,R)-sulphoximine
-
L-methionine-DL-sulfoximine
L-methionine-S-sulfoximine
L-methionine-sulfoximine
-
-
L-Pro
-
weak, gamma-glutamyl transferase activity
L-serine
-
decreases the enzyme activity considerably
L-Tyr
-
inhibits transferase activity, no inhibition of biosynthetic activity
Li+
inhibits the activity of the wild-type enzyme at 1 mM
Met
-
irreversible, competitive
methionine sulfone amine
-
-
N-(1,1-dioxo-1lambda6-thiolan-3-yl)glycine
-
N-(4-hydroxy-3-sulfophenyl)glycine
48% inhibition at 1.0 mM
N-(4-isopropylphenyl)aminomethylenebisphosphonic acid
-
N-(4-methylphenyl)aminoethalidenebisphosphonic acid
-
N-(4-oxo-5,10-dihydro-4H-imidazo[1,2-a]indeno[1,2-e]pyrazin-9-yl)acetamide
-
N-Acetylimidazole
inhibition of isozyme MtGS1a; slight inhibition of isozyme MtGS2a
N-phenylaminoethalidenebisphosphonic acid
-
N-phenylaminomethylenebisphosphonic acid
-
N-[(2S)-2-amino-4-[hydroxy(methyl)phosphoryl]butanoyl]-L-alanyl-L-alanine
-
N-[[(Iodoacetyl)amino]ethyl]-5-naphthylamine-1-sulfonic acid
-
inactivates Mg2+-dependent activity and activates Mn2+-dependent activity
NaNO3
the specific activity of glutamine synthetase is reduced 66% in the presence of NaNO3
nitrogen sensor protein GlnK1
the nitrogen sensor protein GlnK1 of the methanogenic archaeon interacts and forms stable complexes with glutamine synthetase GlnA1. Complex formation with GlnK1 in the absence of metabolites inhibits the activity of GlnA1. The nitrogen sensor GlnK1 allows finetuning control of the glutamine synthetase activity under changing nitrogen availabilities. The following model is proposed: under nitrogen limitation, increasing concentrations of 2-oxoglutarate stimulate maximal GlnA1 activity and transform GlnA1 into an activated conformation, which prevents inhibition by GlnK1. Upon a shift to nitrogen sufficiency after a period of nitrogen limitation, GlnA1 activity is reduced by decreasing internal 2-oxoglutarate concentrations through diminished direct activation and by GlnK1 inhibition
-
O-acetyl-4-phosphonohomoserine
P-ethyl gamma-phosphinic L-glutamate
-
-
P2X7 receptor
-
stimulation of P2X7 receptors for 2 h inhibits both activity and protein expression of glutamine synthetase, periodate-oxidized 2',3'-dialdehyde ATP abolishes the inhibition
-
phenylethylidene-1-hydroxy-1,1-bisphosphonic acid
-
phenylmethylidene-1-hydroxy-1,1-bisphosphonic acid
-
S-nitrosoglutathione
isozyme MtGS2a activity is inhibited by thiol residue nitrosylation
serine
-
more inhibitory for enzyme from strain SA0 than for enzyme from SA1
Snake venom diesterase
-
-
-
sodium gluconate
the specific activity of glutamine synthetase is reduced 34% in the presence of sodium gluconate
sodium nitroprusside
NO donor sodium nitroprusside results in increased in vivo enzyme nitration accompanied by a reduction in enzyme activity; NO donor sodium nitroprusside results in increased in vivo enzyme nitration accompanied by a reduction in enzyme activity
Sulfoxamine
-
irreversible, competitive
Tabtoxinine-beta-lactam
-
-
Tetranitromethane
inhibition of isozyme MtGS1a
thiol reagents
-
suppress activity of enzyme form GS1
thymidine
-
complete inhibition of enzyme form GSII, partial inhibition of enzyme form GSI, no effect on enzyme form GSIII
UMP
-
competitive with respect to L-Gln
Urea
-
physiological concentrations of urea inhibit, at least when ATP and/or glutamate are nonsaturating. Inhibition is partially reversed by trimethylamine-N-oxide
Val
-
inhibition of biosynthetic and transferase activity
vitamin D
-
22% inhibition at 0.00001 mM, reduces dexamethasone induced increase in enzyme expression
[(2-chloro-3-methylphenyl)(hydroxy)methylene]bis(phosphonic acid)
-
[(2-chloroanilino)methylene]bis(phosphonic acid)
-
[(3,4-dichloroanilino)methylene]bis(phosphonic acid)
-
[(3,5-dichloroanilino)methylene]bis(phosphonic acid)
[(3,5-difluoroanilino)methylene]bis(phosphonic acid)
-
[(3,5-dimethylanilino)methylene]bis(phosphonic acid)
-
[(3,5-dimethylphenyl)(hydroxy)methylene]bis(phosphonic acid)
-
[(3-carbamoylanilino)methylene]bis(phosphonic acid)
-
[(3-chloroanilino)methylene]bis(phosphonic acid)
-
[(4-benzylanilino)methylene]bis(phosphonic acid)
-
[(4-benzylphenyl)(hydroxy)methylene]bis(phosphonic acid)
-
[(4-chloroanilino)methylene]bis(phosphonic acid)
-
[(4-methylanilino)methylene]bis(phosphonic acid)
-
[(cyclohexylamino)methanediyl]bis(phosphonic acid)
-
-
[(pyridin-2-ylamino)methanediyl]bis(phosphonic acid)
-
-
[1-amino-3-(S-methylsulfonimidoyl)propyl]phosphonic acid
-
-
[2-(2,3-dichlorophenyl)-1-hydroxyethane-1,1-diyl]bis(phosphonic acid)
-
[2-(2,6-dichloroanilino)ethane-1,1-diyl]bis(phosphonic acid)
-
[2-(2,6-dichlorophenyl)-1-hydroxyethane-1,1-diyl]bis(phosphonic acid)
-
[2-(3,5-dichloroanilino)ethane-1,1-diyl]bis(phosphonic acid)
-
[2-(3,5-dimethylphenyl)-1-hydroxyethane-1,1-diyl]bis(phosphonic acid)
-
[2-(4-benzylanilino)ethane-1,1-diyl]bis(phosphonic acid)
-
[2-(4-chlorophenyl)-1-hydroxyethane-1,1-diyl]bis(phosphonic acid)
-
[2-[(5,6,7,8-tetrahydronaphthalen-1-yl)amino]ethane-1,1-diyl]bis(phosphonic acid)
-
[2-[3,5-bis(trifluoromethyl)anilino]ethane-1,1-diyl]bis(phosphonic acid)
-
[3-(diethoxyphosphoryl)phenylamino]acetic acid
42% inhibition at 1.0 mM
[3-[6-bromo-3-(cyclopentylamino)imidazo[1,2-a]pyridin-2-yl]phenyl]methanol
-
-
[4-(6-methoxynaphthalen-2-yl)-5-(pyridin-4-yl)-1H-imidazol-2-yl]methanol
-
-
[4-[6-bromo-3-(butylamino)imidazo[1,2-a]pyridin-2-yl]phenoxy]acetic acid
-
[[(2,3-dichlorophenyl)amino]methanediyl]bis(phosphonic acid)
non-competitive mechanism against glutamate and uncompetitive mechanism against ATP
[[(2,3-dihydro-1H-inden-5-yl)amino]methylene]bis(phosphonic acid)
-
[[(2,4-dichlorophenyl)amino]methanediyl]bis(phosphonic acid)
non-competitive mechanism against glutamate and uncompetitive mechanism against ATP
[[(2,6-dichlorophenyl)amino]methanediyl]bis(phosphonic acid)
non-competitive mechanism against glutamate and uncompetitive mechanism against ATP
[[(3,5-dichlorophenyl)amino]methanediyl]bis(phosphonic acid)
[[(3-nitrophenyl)amino]methanediyl]bis(phosphonic acid)
-
-
[[(4-chlorophenyl)amino]methanediyl]bis(phosphonic acid)
non-competitive mechanism against glutamate and uncompetitive mechanism against ATP
[[(4-methylphenyl)amino]methanediyl]bis(phosphonic acid)
-
-
[[(5,6,7,8-tetrahydronaphthalen-2-yl)amino]methylene]bis(phosphonic acid)
-
[[(5-chloropyridin-2-yl)amino]methanediyl]bis(phosphonic acid)
-
-
[[(pyridin-2-ylmethyl)amino]methanediyl]bis(phosphonic acid)
-
-
[[3-(trifluoromethyl)anilino]methylene]bis(phosphonic acid)
-
(1R,3R)-1-amino-3-(hydroxy(methyl)phosphoryl)cyclohexanecarboxylic acid
-
-
(1R,3R)-1-amino-3-(hydroxy(methyl)phosphoryl)cyclohexanecarboxylic acid
-
-
(1R,3R)-1-amino-3-(hydroxy(methyl)phosphoryl)cyclohexanecarboxylic acid
Sorghum sp.
-
-
(1R,3R)-1-amino-3-(hydroxy(methyl)phosphoryl)cyclohexanecarboxylic acid
-
-
(1R,3R)-1-amino-3-(hydroxy(methyl)phosphoryl)cyclohexanecarboxylic acid
-
-
(2R,3S)-3-aminooxetane-2-carboxylic acid
-
(2R,3S)-3-aminooxetane-2-carboxylic acid
-
-
(2S)-2-amino-4-(hydroxyamino)butanoic acid
-
-
(2S)-2-amino-4-(hydroxyamino)butanoic acid
-
-
(2S)-2-amino-4-[(1-aminoethyl)(hydroxy)phosphoryl]butanoic acid
-
-
(2S)-2-amino-4-[(1-aminoethyl)(hydroxy)phosphoryl]butanoic acid
-
-
(2S)-2-amino-4-[(aminomethyl)(hydroxy)phosphoryl]butanoic acid
-
-
(2S)-2-amino-4-[(aminomethyl)(hydroxy)phosphoryl]butanoic acid
-
-
(2S)-2-amino-4-[hydroxy(hydroxymethyl)phosphoryl]butanoic acid
-
-
(2S)-2-amino-4-[hydroxy(hydroxymethyl)phosphoryl]butanoic acid
-
-
(R)-methionine sulfoximine phosphate
-
weak inhibition compared to the S-enantiomer
(R)-methionine sulfoximine phosphate
weak inhibition compared to the S-enantiomer
(R)-methionine sulfoximine phosphate
-
weak inhibition compared to the S-enantiomer
(R)-methionine sulfoximine phosphate
-
weak inhibition compared to the S-enantiomer
(R)-methionine sulfoximine phosphate
-
weak inhibition compared to the S-enantiomer
(S)-methionine sulfoximine phosphate
-
irreversible, reaction mechanism with required phosphorylation of the inhibitor molecule in the same way as substrate L-glutamate is phosphorylated
(S)-methionine sulfoximine phosphate
irreversible, reaction mechanism with required phosphorylation of the inhibitor molecule in the same way as substrate L-glutamate is phosphorylated
(S)-methionine sulfoximine phosphate
-
irreversible, reaction mechanism with required phosphorylation of the inhibitor molecule in the same way as substrate L-glutamate is phosphorylated
(S)-methionine sulfoximine phosphate
-
irreversible, reaction mechanism with required phosphorylation of the inhibitor molecule in the same way as substrate L-glutamate is phosphorylated
(S)-methionine sulfoximine phosphate
-
irreversible, reaction mechanism with required phosphorylation of the inhibitor molecule in the same way as substrate L-glutamate is phosphorylated
2-amino-2-ethyl-4-[hydroxy(methyl)phosphoryl]butanoic acid
-
2-amino-2-ethyl-4-[hydroxy(methyl)phosphoryl]butanoic acid
-
-
2-amino-2-ethyl-4-[hydroxy(methyl)phosphoryl]butanoic acid
Sorghum sp.
-
-
2-amino-2-ethyl-4-[hydroxy(methyl)phosphoryl]butanoic acid
-
-
2-amino-4-[(phosphonomethyl)sulfonyl]butanoic acid
-
-
2-amino-4-[(phosphonomethyl)sulfonyl]butanoic acid
-
51% inhibition at 0.5 mM
2-amino-4-[ethyl(hydroxy)phosphoryl]butanoic acid
-
-
2-amino-4-[ethyl(hydroxy)phosphoryl]butanoic acid
-
-
2-amino-4-[hydroxy(phosphonomethyl)phosphoryl]butanoic acid
-
-
2-amino-4-[hydroxy(phosphonomethyl)phosphoryl]butanoic acid
-
-
2-amino-4-[hydroxy(phosphonomethyl)phosphoryl]butanoic acid
-
-
2-mercaptoethanol
-
-
2-mercaptoethanol
-
no inhibition of wild type enzyme, inhibits activity of D56A and D56E mutant enzymes
3-[(phosphonoacetyl)amino]alanine
-
-
3-[(phosphonoacetyl)amino]alanine
-
-
3-[6-bromo-3-(cyclopentylamino)imidazo[1,2-a]pyridin-2-yl]benzoic acid
-
-
3-[6-bromo-3-(cyclopentylamino)imidazo[1,2-a]pyridin-2-yl]benzoic acid
-
3-[6-bromo-3-(cyclopentylamino)imidazo[1,2-a]pyridin-2-yl]phenol
-
-
3-[6-bromo-3-(cyclopentylamino)imidazo[1,2-a]pyridin-2-yl]phenol
-
4-phosphonohomoserine
-
-
4-phosphonohomoserine
-
-
4-phosphonohomoserine
Sorghum sp.
-
-
4-phosphonohomoserine
-
-
4-phosphonohomoserine
-
-
4-phosphononorvaline
-
-
4-phosphononorvaline
Sorghum sp.
-
-
4-[2-tert-butyl-4-(6-methoxynaphthalen-2-yl)-1H-imidazol-5-yl]pyridin-2-amine
-
4-[2-tert-butyl-4-(6-methoxynaphthalen-2-yl)-1H-imidazol-5-yl]pyridin-2-amine
-
-
4-[2-tert-butyl-4-(6-methoxynaphthalen-2-yl)-1H-imidazol-5-yl]pyridin-2-amine
-
4-[2-tert-butyl-4-(6-methoxynaphthalen-2-yl)-1H-imidazol-5-yl]pyridine
-
-
4-[2-tert-butyl-4-(6-methoxynaphthalen-2-yl)-1H-imidazol-5-yl]pyridine
-
4-[hydroxy(methyl)phosphoryl]isovaline
-
-
4-[hydroxy(methyl)phosphoryl]isovaline
-
4-[hydroxy(methyl)phosphoryl]isovaline
-
-
4-[hydroxy(methyl)phosphoryl]isovaline
-
4-[hydroxy(methyl)phosphoryl]isovaline
Sorghum sp.
-
-
4-[hydroxy(methyl)phosphoryl]isovaline
-
-
5'-p-fluorosulfonylbenzoyladenosine
-
Mn2+-dependent activity
5'-p-fluorosulfonylbenzoyladenosine
-
in presence of Mg2+ or Mn2+
5-oxo-6-phosphononorleucine
-
-
5-oxo-6-phosphononorleucine
-
-
5-oxo-6-phosphononorleucine
-
-
5-oxolysine
-
5-oxolysine
-
isozyme GS1; isozyme GS2
5-[6-bromo-3-(cyclopentylamino)imidazo[1,2-a]pyridin-2-yl]-2-methoxyphenol
-
-
5-[6-bromo-3-(cyclopentylamino)imidazo[1,2-a]pyridin-2-yl]-2-methoxyphenol
-
adenosine
-
more potent inhibitor in the reaction with Mg2+ than with Mn2+
adenosine
-
more potent inhibitor in the reaction with Mg2+ than with Mn2+
adenosine
-
more potent inhibitor in the reaction with Mg2+ than with Mn2+
ADP
-
more potent inhibition in the reaction with Mg2+ than with Mn2+
ADP
-
more potent inhibition in the reaction with Mg2+ than with Mn2+
ADP
-
more potent inhibition in the reaction with Mg2+ than with Mn2+
ADP
competitive inhibitor with respect to ATP and noncompetitive inhibitor versus both glutamate and ammonium
ADP
-
biosynthetic activity
ADP
-
strong, enzyme form GSIII
Ala
-
gamma-glutamyl transferase activity
Ala
-
more inhibition by L-Ala and glycine in the mixture with Mn2+ than with Mg2+
Ala
-
more inhibition by L-Ala and glycine in the mixture with Mn2+ than with Mg2+
Ala
-
more inhibition by L-Ala and glycine in the mixture with Mn2+ than with Mg2+
Ala
-
noncompetitive with respect to glutamate
Ala
-
beta-Ala; inhibition of enzyme form GSII and GSIII
Ala
-
strong inhibition of transferase activity
AMP
-
-
AMP
-
more potent inhibitor in the reaction with Mg2+ than with Mn2+
AMP
-
more potent inhibitor in the reaction with Mg2+ than with Mn2+
AMP
-
more potent inhibitor in the reaction with Mg2+ than with Mn2+
AMP
-
competitive with respect to ATP
AMP
-
no feedback inhibition of unadenylated enzyme form, enhanced sensitivity to feedback inhibition by adenylated enzyme form
AMP
-
biosynthetic activity
AMP
slight inhibition of the biosynthetic reaction
Asp
-
-
Asp
-
inhibition of biosynthetic and transferase activity
ATP
-
mutant S186F enzyme is resistant to feedback inhibition by glutamine and AMP
ATP
-
ATP in excess of Mg2+
ATP
-
ATP in excess of Mg2+
ATP
-
biosynthetic reaction
ATP
-
ATP treatment decreases glutamine synthetase activities and protein expression
Ca2+
-
-
Ca2+
-
strong inhibition of Mg2+-activated enzyme
Ca2+
-
above 2 mM CaCl2, in presence of 20 mM MgCl2 and 10 mM ATP
Ca2+
-
inhibits in presence of Mg2+
Ca2+
inhibitory effect on Mg2+-driven activity
Carbamoyl phosphate
-
-
Carbamoyl phosphate
-
non-competitive with respect to L-Glu
Co2+
-
0.5-60 mM, inhibition of Mn2+-dependent transferase activity
Co2+
inhibits the activity of the wild-type enzyme at 1 mM
Co2+
-
strong inhibition of Mg2+-activated enzyme
CTP
-
biosynthetic reaction
CTP
-
no feedback inhibition of unadenylated enzyme form, enhanced sensitivity to feedback inhibition by adenylated enzyme form
Cu2+
-
-
Cu2+
Cu2+ strongly inhibits the activity of wild-type and mutant enzymes at 1 mM
cysteine
-
no inhibition of wild type enzyme, inhibits activity of D56A and D56E mutant enzymes
cysteine
-
more inhibitory for enzyme from strain SA0 than for enzyme from SA1
D-Methionine sulfone
-
-
diphosphate
-
-
diphosphate
-
enzyme form GSIII
Fe2+
-
-
GDP
-
weak
glucagon
-
slightly decreases enzyme activity
glucagon
-
slightly decreases enzyme activity
glucagon
-
slightly decreases enzyme activity
glucagon
-
slightly decreases enzyme activity
glutamate
at high concentrations, isoenzyme GLN1,3
glutamate
-
product inhibition above 20 mM when enzyme is activated with Mg2+, no inhibition when activated with Mn2+
glutamine
-
feed-back inhibition of wild-type enzyme, mutant S186F enzyme is resistant to feedback inhibition
glutamine
2.5 mM, 50% inhibition
Gly
-
gamma-glutamyl transferase activity
Gly
-
more inhibition by L-Ala and Gly in the mixture with Mn2+ than with Mg2+
Gly
-
more inhibition by L-Ala and Gly in the mixture with Mn2+ than with Mg2+
Gly
-
more inhibition by L-Ala and Gly in the mixture with Mn2+ than with Mg2+
Gly
-
inhibition of biosynthetic and transferase activity
glycine
-
-
glycine
feed-back inhibition, competitive with L-glutamine
glycine
-
more inhibitory for enzyme from strain SA0 than for enzyme from SA1
H2O2
inhibits isozyme MtGS2a
H2O2
-
1 mM, 3 h, 63% loss of activity. Inactivation is prevented by the iron chelators 2,2'-dipyridylor 1,10-phenanthroline, but not by their non-chelating analogues
H2O2
-
1 mM, 30 min, 41% loss of activity. Complete inactivation by co-incubation with 1 mM H2O2, 0.002 mM Fe3+, 2 mM ascorbate for 30 min
Hg2+
-
-
His
-
L-His, gamma-glutamyl transferase activity
His
-
no feedback inhibition of unadenylated enzyme form, enhanced sensitivity to feedback inhibition by adenylated enzyme form
L-alanine
-
decreases the enzyme activity considerably
L-alanine
feed-back inhibition, competitive with L-glutamine
L-Arg
-
gamma-glutamyl transferase activity
L-Arg
-
biosynthetic activity
L-Glu
-
gamma-glutamyl transferase activity
L-Glu
-
competitive versus L-Gln and non-competitive versus hydroxylamine; gamma-glutamyl transferase activity
L-Glu
-
inhibition of transferase activity, no inhibition of biosynthetic activity
L-Glu
-
50-100 mM, substrate inhibition
L-glutamine
-
inhibitory at high concentrations
L-glutamine
-
the enzyme is feedback inhibited
L-glutamine
-
the enzyme is feedback inhibited, the feedback inhibition of GS induces the sequence-specific binding of transcription factor GlnR to DNA in nitrogen metabolism regulation by 32fold and reduces the dissociation rate by 18fold stabilizing the complexes, overview
L-glutamine
-
feedback inhibition
L-glutamine
feedback inhibition of isozymes GSI-alpha and GSI-beta. Feedback inhibition arises from a hydrogen bond network between Gln, the catalytic glutamate, and the GSI-alpha-specific residue, Arg62, from an adjacent subunit. Arg62 must be ejected for proper active site reorganization. An R62A mutation abrogates Gln feedback inhibition but does not affect catalysis
L-glutamine
noncompetitive
L-glutamyl gamma-phosphinic acid
-
-
L-glutamyl gamma-phosphinic acid
-
-
L-Ile
-
weak, gamma-glutamyl transferase activity
L-Lys
-
no inhibition
L-methionine sulfone
-
L-methionine sulfone
-
inhibits enzyme from strain SA0 but not from SA1, more than 80% inhibition at 0.05 mM
L-methionine sulfoximine
-
gamma-glutamyl transferase assay
L-methionine sulfoximine
-
-
L-methionine sulfoximine
-
loss of glutamine synthetase activity either inherited or induced through L-methionine sulfoximine leads to an upregulation of the glutamine synthetase protein but not of the glutamine synthetase mRNA and results in a significant drop in the proliferation rate but has no effect on apoptosis
L-methionine sulfoximine
-
-
L-methionine sulfoximine
-
L-methionine sulfoximine
-
-
L-methionine sulfoximine
-
L-methionine sulfoximine
-
no inhibition of the acetyltransferase activity
L-methionine sulfoximine
-
forward reaction: complete inhibition of wild type enzyme, only slight inhibition of mutant enzyme, reverse reaction: slight inhibition of mutant and wild-type enzyme
L-methionine sulfoximine
-
-
L-methionine sulfoximine
-
irreversible at high concentrations, competitive with L-Glu; S,R-sulfoximine and S-sulfoximine inhibit, R-sulfoximine is ineffective
L-methionine sulfoximine
-
-
L-methionine sulfoximine
-
inhibition of enzyme form GSII and GSIII
L-methionine sulfoximine
-
-
L-methionine sulfoximine
-
the concentration needed to inhibit GSIII is 50-100times higher than that needed to inhibit GSI or GSII
L-methionine sulfoximine
-
-
L-methionine sulfoximine
-
-
L-methionine sulfoximine
-
enzyme form GS III
L-methionine sulfoximine
50% inhibition at 47 mM
L-methionine-DL-sulfoximine
-
complete inhibition
L-methionine-DL-sulfoximine
MSX, complete inactivation of wild-type and mutant enzymes except D51E mutant, which shows only 10% inhibition
L-methionine-DL-sulfoximine
-
inhibits enzyme from strain SA0 but not from SA1, more than 80% inhibition at 0.05 mM
L-methionine-S-sulfoximine
-
-
L-methionine-S-sulfoximine
-
-
L-methionine-S-sulfoximine
-
L-phosphinothricin
the glutamine synthetase from Exiguobacterium sp. is L-phosphinothricin resistant. Molecular docking analysis indicates that the substitution of residues Glu60 and Arg64 may lead to significant changes in binding pocket
L-phosphinothricin
50% inhibition at 0.5 mM
methionine sulfoxide
-
-
methionine sulfoximine
-
2.5 mM causes up to 60% inhibition of the transferase GS activity and in the presence of 6 mM, the transferase GS activity is around 20% of the controls
methionine sulfoximine
-
an irreversible, competitive inhibitor of glutamine synthetase activity
methionine sulfoximine
-
-
methionine sulfoximine
-
treatment with methionine sulfoximine of transgenic mice that overexpresses the mutant human superoxide dismutase SOD1G93A gene, an animalmodel for the primary inherited form of the human neurodegenerative disease amyotrophic lateral sclerosis. This treatment in vivo reduces glutamine synthetase activity measured in vitro by 85% and reduces brain levels of glutamine by 60% and of glutamate by 30% in both the motor cortex and the anterior striatum, while also affecting levels of GABA and glutathione. Methionine sulfoxime treatment significantly extends the lifespan of these mice by 8%
methionine sulfoximine
MSO, originally isolated from the maize protein zein after treatment with nitrogen trichloride, targets the amino acid-binding site of the enzyme. Treatment of Mycobacterium tuberculosis with MSO inhibits both cell wall formation and bacterial growth. MSO initially binds as a competitive inhibitor and undergoes rapid phosphorylation by the glutamate synthetase, producing the active form, methionine sulfoximine phosphate (MSO-P). MSO-P binds essentially irreversibly to the active site, preventing entry of the glutamate substrate. The configuration of the two stereocenters is important for inhibitory activity. The (S,S)-diastereomer is 10times more potent than the (S,R)-isomer
methionine sulfoximine
-
-
methionine sulfoximine
-
-
methionine sulfoximine
-
irreversible inhibition up to 97% in vivo after longterm treatment over 3 h by Intracranial infusion
methionine sulfoximine
-
-
methionine sulfoximine
competitive inhibitor with respect to L-glutamate
Mg2+
-
above 0.5 mM, gamma-glutamyl transferase activity
Mg2+
-
in gamma-glutamyl transferase assay
Mg2+
-
between 0.5-60 mM, inhibition of Mn2+-dependent transferase activity
Mg2+
-
addition of Mg2+ to the Mn2+-dependent transferase activity
Mg2+
activiation up to 25 mM, inhibition above
Mg2+
-
inhibits gamma-glutamyl transferase activity
Mg2+
-
inhibition at more than 20 mM excess of MgCl2 over ATP
Mg2+
-
inhibits enzyme form GSIII to nearly 72%, enzyme form GSI 30%, and enzyme form GSII 33.3%
Mn2+
-
strong inhibition of Mg2+-activated enzyme
Mn2+
-
above 2 mM MnCl2, in presence of 20 mM MgCl2 and 10 mM ATP
Mn2+
-
inhibitory for enzyme from strain SA0
NaCl
-
0.25 mM decreases GS activity to 29.9% in leaves, 40% in roots
NaCl
-
84.11% decrease of activity at 300 mM
NH4+
-
in the presence of Mn2+ the activity decreases when exceeding a concentration of 20 mM NH4+
NH4+
inhibits the activity of the wild-type enzyme at 1 mM
NH4+
-
reversible inactivation
NH4Cl
-
glutamyl transferase reaction, competitive versus L-Gln and non-competitive versus hydroxylamine
NH4Cl
-
substrate inhibition at high concentrations
Ni2+
-
-
Ni2+
-
0.5-60 mM, inhibition of Mn2+-dependent transferase activity
Ni2+
inhibits the activity of the wild-type enzyme at 1 mM
Ni2+
-
higher affinity for nickel than for the regular co-factor manganese. Upon binding, nickel interferes with the manganese-catalyzed enzymatic activity of recombinant GLUL protein. GLUL activity in testes of animals exposed to nickel sulfate is reduced
nitrogen
-
the activity of GlnA1 is downregulated under conditions of nitrogen excess, through covalent binding of an AMP-moiety to a conserved Tyr405 residue by GlnE, an adenylyltransferase
nitrogen
-
the activity of GlnA1 is downregulated under conditions of nitrogen excess, through covalent binding of an AMP-moiety to a conserved Tyr405 residue by GlnE, an adenylyltransferase
nitrogen
the activity of GlnA1 is downregulated under conditions of nitrogen excess, through covalent binding of an AMP-moiety to a conserved Tyr405 residue by GlnE, an adenylyltransferase. Both GSII activity and glnII transcription levels increase during nitrogen starvation of morphologically differentiating cultures while there was no change in glnA1 transcription
O-acetyl-4-phosphonohomoserine
-
-
O-acetyl-4-phosphonohomoserine
Sorghum sp.
-
-
p-hydroxymercuribenzoate
-
complete inhibition of wild type and D56A mutant, 40% inhibition of D56E at 1 mM
p-hydroxymercuribenzoate
-
biosynthetic activity
peroxynitrite
inhibition of isozyme MtGS1a
peroxynitrite
-
0.005 mM, activity is decreased by about 25%
peroxynitrite
-
0.005 mM, inactivation of the enzyme
phosphate
noncompetitive
phosphate
-
transferase assay an biosynthetic assay
Phosphinothricin
-
isolated from Streptomyces viridochromogenes
Phosphinothricin
-
isolated from Streptomyces viridochromogenes
Phosphinothricin
-
i.e. L-2-amino-4-(hydroxymethyl-phosphinyl)butanoic acid, competitive with respect to Glu, reversible first order inactivation
Phosphinothricin
-
mechanism of inactivation
Phosphinothricin
-
isolated from Streptomyces viridochromogenes
Phosphinothricin
isolated from Streptomyces viridochromogenes; isolated from Streptomyces viridochromogenes
Phosphinothricin
targets the amino acid-binding site of the enzyme
Phosphinothricin
-
isolated from Streptomyces viridochromogenes
Phosphinothricin
-
isolated from Streptomyces viridochromogenes
Phosphinothricin
isolated from Streptomyces viridochromogenes
Phosphinothricin
-
isolated from Streptomyces viridochromogenes
Phosphinothricin
Sorghum sp.
-
isolated from Streptomyces viridochromogenes
Phosphinothricin
-
irreversible, competitive
Phosphinothricin
-
isolated from Streptomyces viridochromogenes
Phosphinothricin
PPT, complete inactivation of wild-type and mutant enzymes except D51E mutant, which shows 70% inhibition
Phosphinothricin
-
isolated from Streptomyces viridochromogenes
Phosphinothricin
-
isolated from Streptomyces viridochromogenes
Phosphinothricin
-
isolated from Streptomyces viridochromogenes
Ser
-
-
Ser
-
inhibition of biosynthetic and transferase activity
Trp
-
-
Trp
-
no feedback inhibition of unadenylated enzyme form, enhanced sensitivity to feedback inhibition by adenylated enzyme form
UTP
-
biosynthetic reaction
Zn2+
-
-
Zn2+
-
0.5-60 mM, inhibition of Mn2+-dependent transferase activity
Zn2+
inhibits the activity of the wild-type enzyme at 1 mM
[(3,5-dichloroanilino)methylene]bis(phosphonic acid)
-
[(3,5-dichloroanilino)methylene]bis(phosphonic acid)
-
-
[[(3,5-dichlorophenyl)amino]methanediyl]bis(phosphonic acid)
-
-
[[(3,5-dichlorophenyl)amino]methanediyl]bis(phosphonic acid)
non-competitive mechanism against glutamate and uncompetitive mechanism against ATP
additional information
-
presence of only one glutathione synthetase inactivation factor, 7A, encoded by open reading frame asl2329, gifA, in strain PCC 7120. Upon addition of ammonium, expression of gifA is derepressed, leading to the synthesis of IF7A, and consequently, glutathione synthetase is inactivated. Upon ammonium removal, the glutathione synthetase activity returns to the initial level and IF7A becomes undetectable. Anabaena glutathione synthetase is not inactivated by Synechocystis IFs. In an Anabaena strain expressing a second inactivating factor, containing the amino-terminal part of IF17 from Synechocystis fused to IF7A, glutathione synthetase inactivation is more effective than that in the wild-ype and resembles that observed in Synechocystis
-
additional information
structure-activity relationships and inhibitor design, overview
-
additional information
-
Bacillus fragilis enzyme produced in E. coli is specifically and irreversibly inactivated by Bacillus fragilis cell extract
-
additional information
-
structure-activity relationships and inhibitor design, overview
-
additional information
-
structure-activity relationships and inhibitor design, overview
-
additional information
design and construction of structure-based inhibitors targeting the nucleotide binding site, which varies to a large degree between mammalian and bacterial enzymes
-
additional information
-
design and construction of structure-based inhibitors targeting the nucleotide binding site, which varies to a large degree between mammalian and bacterial enzymes
-
additional information
-
structure-activity relationships and inhibitor design, overview
-
additional information
-
structure-activity relationships and inhibitor design, overview
-
additional information
-
a single transcriptional repressor AmtR from the TetR family is involved in enzyme regulation, AmtB is encoded by amtB clustered together with glnK in an operon, glnK encodes for a PII signaling protein which are small trimeric proteins that are able to bind 2-oxoglutarate and play a pivotal role in the regulation of nitrogen metabolism by way of controlling the activity of signal transduction components and key metabolic enzymes. GlnK is not uridylylated but rather adenylylated/de-adenylylated by GlnD
-
additional information
-
inactivation by ADP-ribosylation. The site of ADP-ribosylation is Arg172
-
additional information
-
structure-activity relationships and inhibitor design, overview
-
additional information
enzyme inactivation by ferric chloride reagent (0.2 M FeCl3, 0.12 M trichloroacetic acid, and 2.1% concentrated HCl). Enzyme oxidative inactivation by three different metal-catalyzed oxidation (MCO) systems, composed of air, FeCl3 and reducing agents (DTT, ascorbate or GSH), overview; enzyme inactivation by ferric chloride reagent (0.2 M FeCl3, 0.12 M trichloroacetic acid, and 2.1% concentrated HCl). Enzyme oxidative inactivation by three different metal-catalyzed oxidation (MCO) systems, composed of air, FeCl3 and reducing agents (DTT, ascorbate or GSH), overview
-
additional information
enzyme inactivation by ferric chloride reagent (0.2 M FeCl3, 0.12 M trichloroacetic acid, and 2.1% concentrated HCl). Enzyme oxidative inactivation by three different metal-catalyzed oxidation (MCO) systems, composed of air, FeCl3 and reducing agents (DTT, ascorbate or GSH), overview; enzyme inactivation by ferric chloride reagent (0.2 M FeCl3, 0.12 M trichloroacetic acid, and 2.1% concentrated HCl). Enzyme oxidative inactivation by three different metal-catalyzed oxidation (MCO) systems, composed of air, FeCl3 and reducing agents (DTT, ascorbate or GSH), overview
-
additional information
-
the canonical Wnt signalling pathway is a negative regulator of glutamine synthetase activity; the canonical Wnt signalling pathway is a negative regulator of glutamine synthetase activity. No effects by aldosterone, estradiol, progesterone, dihydrotestosterone, or triiodothyronine
-
additional information
-
elevations in c-jun may be a potential cause of the glutamine synthetase deficiency in mesial temporal lobe epilepsy, MTLE. The activity of glutamine synthetase is decreased by 38% in tissue homogenates of the sclerotic versus the nonsclerotic hippocampus. High levels of c-jun repress the glutamine synthetase gene. The inductive effect of glucocorticoids is mediated by binding of the glucocorticoi receptor to a glucocorticoid response element in the regulatory region of the glutamine synthetase gene, and this effect is blocked by the proinflammatory cytokines interleukin-1beta and tumor necrosis factor-alpha
-
additional information
-
design and construction of structure-based inhibitors targeting the nucleotide binding site, which varies to a large degree between mammalian and bacterial enzymes
-
additional information
structure-activity relationships and inhibitor design, overview
-
additional information
-
structure-activity relationships and inhibitor design, overview; structure-activity relationships and inhibitor design, overview
-
additional information
structure-activity relationships and inhibitor design, overview; structure-activity relationships and inhibitor design, overview
-
additional information
-
combined inhibition by Gly, Ala and Ser is cumulative
-
additional information
no inhibition by H2O2 and S-nitrosoglutathione, epicatechin is able to protect isozyme MtGS1a from inactivation; no inhibition by iodoacetamide, epicatechin is not able to protect isozyme MtGS2a from inactivation
-
additional information
no inhibition by H2O2 and S-nitrosoglutathione, epicatechin is able to protect isozyme MtGS1a from inactivation; no inhibition by iodoacetamide, epicatechin is not able to protect isozyme MtGS2a from inactivation
-
additional information
-
no inhibition by H2O2 and S-nitrosoglutathione, epicatechin is able to protect isozyme MtGS1a from inactivation; no inhibition by iodoacetamide, epicatechin is not able to protect isozyme MtGS2a from inactivation
-
additional information
-
the enzyme is not affeted by dietary glutamine supplementation or by Mycobacterium bovis bacillus Calmette-Guerin infection, overview
-
additional information
structure-activity relationships and inhibitor design, overview
-
additional information
no inhibition by L-homoserine, (R)-3-hydroxy-2-(3-methanesulfinylphenylamino)propionic acid, (R)-3-hydroxy-2-(3-methylsulfanylphenylamino)propionic acid, (3-sulfamoylphenylamino)acetic acid, (3-methylsulfanylphenylamino)acetic acid, 2-amino-3-(2-phosphonomethylphenyl)propanoic acid, 2-amino-3-(2-aminomethylphenyl)propanoic acid, and methyl 2-amino-3-(2-phosphonomethylphenyl)propanoate, inhibitor screening and docking studies, overview
-
additional information
-
no inhibition by L-homoserine, (R)-3-hydroxy-2-(3-methanesulfinylphenylamino)propionic acid, (R)-3-hydroxy-2-(3-methylsulfanylphenylamino)propionic acid, (3-sulfamoylphenylamino)acetic acid, (3-methylsulfanylphenylamino)acetic acid, 2-amino-3-(2-phosphonomethylphenyl)propanoic acid, 2-amino-3-(2-aminomethylphenyl)propanoic acid, and methyl 2-amino-3-(2-phosphonomethylphenyl)propanoate, inhibitor screening and docking studies, overview
-
additional information
-
a single transcriptional repressor AmtR from the TetR family is involved in enzyme regulation, AmtB is encoded by amtB clustered together with glnK in an operon, glnK encodes for a PII signaling protein which are small trimeric proteins that are able to bind 2-oxoglutarate and play a pivotal role in the regulation of nitrogen metabolism by way of controlling the activity of signal transduction components and key metabolic enzymes. GlnK is not uridylylated but rather adenylylated/de-adenylylated by GlnD
-
additional information
structure-activity relationships and inhibitor design, overview
-
additional information
-
synthesis and inhibitory potency of 2-tert-butyl-4,5-diarylimidazoles inhibitors, overview. No inhibition by 4-[4-(6-methoxynaphthalen-2-yl)-2-(phenoxymethyl)-1H-imidazol-5-yl]pyridine and [4-(6-methoxynaphthalen-2-yl)-5-(pyridin-4-yl)-1H-imidazol-2-yl]methanol
-
additional information
high throughput screening of series of imidazo[1,2-a]indeno[1,2-e]pyrazin-4-ones as enzyme inhibitors, overview. None of these compounds is active on whole cell Mycobacterium tuberculosis. Structure activity relationships of 5,10-dihydro-imidazo[1,2-a]indeno[1,2-e]pyrazin-4-one derivatives
-
additional information
-
high throughput screening of series of imidazo[1,2-a]indeno[1,2-e]pyrazin-4-ones as enzyme inhibitors, overview. None of these compounds is active on whole cell Mycobacterium tuberculosis. Structure activity relationships of 5,10-dihydro-imidazo[1,2-a]indeno[1,2-e]pyrazin-4-one derivatives
-
additional information
43 bisphosphonic and bis-H-phosphinic acids of various scaffolds, bearing aromatic substituents, are synthesized and screened against recombinant enzyme from Mycobacterium tuberculosis. Some of the inhibitors are much more effective against the pathogen enzyme than against the human orthologue. Bone-targeting properties of the bisphosphonate compounds. No inhibition by [(3,5-dibromoanilino)methylene]bis(phosphonic acid), [[3,5-bis(trifluoromethyl)anilino]methylene]bis(phosphonic acid), (anilinomethylene)di(lambda5-phosphanedione), [(4-methylanilino)methylene]di(lambda5-phosphanedione), [(3,5-dichloroanilino)methylene]di(lambda5-phosphanedione), and [(4-benzylanilino)methylene]di(lambda5-phosphanedione). Molecular modeling
-
additional information
-
43 bisphosphonic and bis-H-phosphinic acids of various scaffolds, bearing aromatic substituents, are synthesized and screened against recombinant enzyme from Mycobacterium tuberculosis. Some of the inhibitors are much more effective against the pathogen enzyme than against the human orthologue. Bone-targeting properties of the bisphosphonate compounds. No inhibition by [(3,5-dibromoanilino)methylene]bis(phosphonic acid), [[3,5-bis(trifluoromethyl)anilino]methylene]bis(phosphonic acid), (anilinomethylene)di(lambda5-phosphanedione), [(4-methylanilino)methylene]di(lambda5-phosphanedione), [(3,5-dichloroanilino)methylene]di(lambda5-phosphanedione), and [(4-benzylanilino)methylene]di(lambda5-phosphanedione). Molecular modeling
-
additional information
in contrast to methionine sulfoximine, MSO, the sulfone and sulfoxide analogues are weak, reversible enzyme inhibitors. Poor or no inhibition by 2-amino-4-(ethanesulfonyl)butanoic acid and amino[3-(methanesulfonyl)phenyl]acetic acid
-
additional information
-
in contrast to methionine sulfoximine, MSO, the sulfone and sulfoxide analogues are weak, reversible enzyme inhibitors. Poor or no inhibition by 2-amino-4-(ethanesulfonyl)butanoic acid and amino[3-(methanesulfonyl)phenyl]acetic acid
-
additional information
-
structure-activity relationships and inhibitor design, overview
-
additional information
-
structure-activity relationships and inhibitor design, overview
-
additional information
-
structure-activity relationships and inhibitor design, overview
-
additional information
-
3'-O-(4-benzoylbenzoyl)-ATP suppresses the enzyme expression. Removal of extracellular Ca2+ and inhibition of protein kinase C restores the ATP-decreased enzyme expression but fails to restore the P2X7-decreased L-glutamate uptake
-
additional information
-
inhibitory effects of endothelins on the expression of glutamine synthetase, cultured cortical astrocytes maintained with endothelins show an almost complete loss of glutamine synthetase, this coordinated inhibition of astroglial glutamate uptake and turnover, e.g. by ET-1, dissociates when extracellular glutamate concentrations increase, overview
-
additional information
structure-activity relationships and inhibitor design, overview
-
additional information
structure-activity relationships and inhibitor design, overview
-
additional information
-
structure-activity relationships and inhibitor design, overview
-
additional information
Sorghum sp.
-
structure-activity relationships and inhibitor design, overview
-
additional information
-
structure-activity relationships and inhibitor design, overview
-
additional information
GlnR is able to function as both an activator and repressor of transcription
-
additional information
-
GlnR is able to function as both an activator and repressor of transcription
-
additional information
no effect with L-histidine or L-tryptophane
-
additional information
-
no effect with L-histidine or L-tryptophane
-
additional information
structure-activity relationships and inhibitor design, overview
-
additional information
-
structure-activity relationships and inhibitor design, overview
-
additional information
-
structure-activity relationships and inhibitor design, overview
-
additional information
-
structure-activity relationships and inhibitor design, overview
-
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175
3-aminopentanedioate
-
pH 7.0, 37°C
0.35 - 62.5
hydroxylamine
2.8
NH4Cl
-
second value 8.9 mM, biphasic plot
additional information
hydroxylamine
0.0000597
ADP
-
gamma-glutamyl transferase assay
0.00091
ADP
pH 6.0, 35°C, recombinant mutant R64G
0.00461
ADP
pH 6.0, 35°C, recombinant mutant E60A
0.00865
ADP
pH 6.0, 35°C, recombinant wild-type enzyme
0.01
ADP
-
transferase activity
0.0113
ADP
pH 6.0, 35°C, recombinant mutant E60A/R64G
0.09
ADP
pH 6.4, 37°C, wild-type enzyme
0.05
ATP
D51A mutant, pH 7.0, 30°C
0.06
ATP
-
isozyme GSIII-1, pH 6.0, 37°C, gamma-glutamylhydroxamate synthetase activity
0.07
ATP
D51S mutant, pH 7.0, 30°C
0.07
ATP
-
isozyme GSIII-2, pH 6.0, 37°C, gamma-glutamylhydroxamate synthetase activity
0.1
ATP
-
enzyme from strain SA0, pH 6.8
0.12
ATP
D51N mutant, pH 7.0, 30°C
0.13
ATP
-
enzyme from strain SA0, pH 7.5
0.17
ATP
-
enzyme from strain SA1, pH 6.8
0.2
ATP
-
wild-type enzyme
0.2
ATP
-
in the presence of Mg2+
0.21
ATP
-
enzyme from strain SA1, pH 7.5
0.21
ATP
wild type enzyme, pH 7.0, 30°C
0.22
ATP
-
biosynthetic assay
0.25
ATP
-
oxidized mutant enzyme E165C
0.26
ATP
-
reduced mutant enzyme E165C
0.3
ATP
-
wild type enzyme, pH 7.5, 37°C
0.3
ATP
-
wild-type and mutant enzyme, pH 7.5, 37°C
0.3
ATP
pH 7.8, 30°C, isoenzyme GLN1,1
0.38
ATP
recombinant enzyme, coupled reactions assay, pH and temperature not specified in the publication
0.39
ATP
recombinant enzyme, Malachite green assay, pH and temperature not specified in the publication
0.43
ATP
-
enzyme form GSIII
0.45
ATP
30°C, isoenzyme OsGLN1,1
0.45
ATP
-
isozyme GSI, pH 6.0, 37°C, gamma-glutamylhydroxamate synthetase activity
0.53
ATP
-
biosynthetic assay, Mg2+-activated, enzyme form EII
0.53
ATP
30°C, isoenzyme OsGLN1,2
0.56
ATP
pH 7.8, 30°C, isoenzyme GLN1,4
0.85
ATP
pH 7.8, 30°C, isoenzyme GLN1,3
1
ATP
-
D56E mutant enzyme, pH 7.5, 37°C
1.1
ATP
pH 7.8, 30°C, isoenzyme GLN1,2
1.2
ATP
-
mutant E304H, 25°C, pH not specified in the publication
1.2
ATP
pH 7.0, temperature not specified in the publication, mutant E304A
1.3
ATP
-
short isoform, pH 7.2, 37°C
1.3
ATP
-
pH 11.0, 30 mM Mg2+
1.4
ATP
-
pH 8.0, 3 mM Mn2+
1.4
ATP
-
pH 8.5, 30 mM Mg2+
1.5
ATP
-
Mg2+-stimulated
1.5
ATP
-
ATP, biosynthetic assay, Mn2+-activated, enzyme form EII
1.5
ATP
-
pH 7.5, 3 mM MN2+
1.5
ATP
-
pH 8.5, 3 mM Mn2+
1.6
ATP
-
D56A mutant enzyme, pH 7.5, 37°C
1.7
ATP
-
Mg2+-stimulated
1.8
ATP
-
synthetase assay
1.83
ATP
pH not specified in the publication, 30°C, wild-type mature enzyme
1.9
ATP
-
long isoform, pH 7.2, 37°C
1.91
ATP
-
isozyme GSIII-1, pH 7.5, 37°C, glutamine synthetase activity
1.95
ATP
pH not specified in the publication, 30°C, mutant mature enzyme lacking the C-terminal peptide
2
ATP
-
Mg2+-stimulated or Mn2+-stimulated
2
ATP
-
pH 8.0, 30 mM Mg2+
2.3
ATP
-
Mn2+-stimulated
2.3
ATP
-
ATP, Mg2+-stimulated
2.3
ATP
pH 7.0, temperature not specified in the publication, mutant R62A
2.4
ATP
-
wild-type enzyme
2.4
ATP
-
wild-type, 25°C, pH not specified in the publication
2.4
ATP
pH 7.0, temperature not specified in the publication, wild-type enzyme
2.5
ATP
-
L-Glu, Mg2+-stimulated
2.5
ATP
-
Mn2+-stimulated
2.5
ATP
-
mutant enzyme S186F
2.65
ATP
-
isozyme GSIII-2, pH 7.5, 37°C, glutamine synthetase activity
2.9
ATP
-
biosynthetic assay, Mg2+-activated, enzyme form EI
2.9
ATP
-
phosphorylated GS1a, in the presence of 0.0005 mM microcystin
3
ATP
-
chloroplast enzyme
3
ATP
-
non-phosphorylated GS1a, in the presence of 0.0005 mM microcystin
4.5
ATP
pH 6.4, 37°C, wild-type enzyme
5.3
ATP
-
mutant G302A, 25°C, pH not specified in the publication
6.45
ATP
pH 6.4, 37°C, mutant enzyme E380A
9.4
ATP
-
mutant Y303H, 25°C, pH not specified in the publication
10.6
ATP
D51E mutant, pH 7.0, 30°C
11
ATP
-
mutant E304D, 25°C, pH not specified in the publication
500
ethylamine
-
pH 8.5, 3 mM Mn2+
700
ethylamine
-
pH 11.0, 30 mM Mg2+
4.9
Gln
-
-
11.6
Gln
-
glutamyl transferase reaction
37.6
Gln
-
transferase assay
48.6
Gln
-
gamma-glutamyl transferase assay
0.9
Glu
-
enzyme form GSIII
3
Glu
-
ATP, biosynthetic assay, Mn2+-activated, enzyme form EI
6.3
Glu
-
biosynthetic assay
6.7
Glu
-
synthetase assay
8.58
Glu
-
biosynthetic assay
13.3
Glu
-
enzyme form GSIII
14
Glu
-
hydroxylamine, glutamyl transferase assay
1.4
glutamate
-
enzyme from strain SA0, pH 6.8
1.7
glutamate
-
enzyme from strain SA0, pH 7.5
5.71
glutamate
-
pH 7.4, 35°C
9.2
glutamate
-
enzyme from strain SA1, pH 6.8
16.8
glutamate
-
enzyme from strain SA1, pH 7.5
0.35
hydroxylamine
-
Mn2+-activated, enzyme form EII
0.4
hydroxylamine
-
Mn2+-activated, enzyme form EI
0.68
hydroxylamine
-
mutant E304H, 25°C, pH not specified in the publication
0.68
hydroxylamine
pH 7.0, temperature not specified in the publication, mutant E304A
0.74
hydroxylamine
-
mutant E304D, 25°C, pH not specified in the publication
0.83
hydroxylamine
-
wild-type, 25°C, pH not specified in the publication
0.83
hydroxylamine
pH 7.0, temperature not specified in the publication, wild-type enzyme
0.85
hydroxylamine
pH not specified in the publication, 30°C, mutant mature enzyme lacking the C-terminal peptide
0.92
hydroxylamine
pH not specified in the publication, 30°C, wild-type mature enzyme
1.04
hydroxylamine
-
isozyme GSIII-1, pH 6.0, 37°C, gamma-glutamylhydroxamate synthetase activity
1.4
hydroxylamine
pH 7.0, temperature not specified in the publication, mutant R62A
1.5
hydroxylamine
pH 6.4, 37°C, mutant enzyme E380A
1.92
hydroxylamine
-
isozyme GSIII-2, pH 6.0, 37°C, gamma-glutamylhydroxamate synthetase activity
2.6
hydroxylamine
-
glutamyltransferase reaction
2.7
hydroxylamine
-
isozyme GSI, pH 6.0, 37°C, gamma-glutamylhydroxamate synthetase activity
2.9
hydroxylamine
-
wild-type enzyme
3.37
hydroxylamine
-
gamma-glutamyl transferase assay
3.4
hydroxylamine
-
mutant enzyme S186F
4.1
hydroxylamine
-
transferase reaction
4.7
hydroxylamine
pH 6.4, 37°C, wild-type enzyme
5.3
hydroxylamine
-
enzyme form GSIII
6
hydroxylamine
-
transferase activity
8.3
hydroxylamine
-
pH 7.0
10.5
hydroxylamine
-
at 45°C
11.1
L-Gln
-
glutamyl transferase reaction
12
L-Gln
-
transferase activity
12.6
L-Gln
-
biosynthetic reaction
22.2
L-Gln
-
transferase reaction
0.0025
L-Glu
-
in the presence of Mg2+
0.67
L-Glu
isoenzyme GLN1,4
0.83
L-Glu
mutant A174S of isoenzyme GLN1,4
1.1
L-Glu
-
Mg2+-stimulated
1.14
L-Glu
mutant K49Q of isoenzyme GLN1,4
1.3
L-Glu
-
Mn2+-stimulated
1.43
L-Glu
mutant K49Q/A174S of isoenzyme GLN1,4
1.8
L-Glu
-
phosphorylated GS1a, in the presence of 0.0005 mM microcystin
2.1
L-Glu
-
Mn2+-stimulated
2.1
L-Glu
-
Gln, transferase reaction
2.1
L-Glu
30°C, isoenzyme OsGLN1,2
2.4
L-Glu
mutant K49Q/A174S of isoenzyme GLN1,3
2.8
L-Glu
-
non-phosphorylated GS1a, in the presence of 0.0005 mM microcystin
3.2
L-Glu
mutant A174S of isoenzyme GLN1,3
3.2
L-Glu
mutant K49Q of isoenzyme GLN1,3
3.3
L-Glu
-
wild-type enzyme
3.4
L-Glu
-
synthetase reaction
4.17
L-Glu
isoenzyme GLN1,3
6
L-Glu
-
oxidized mutant enzyme E165C
7
L-Glu
-
reduced mutant enzyme E165C
17
L-Glu
-
biosynthetic assay, Mg2+-activated, enzyme form I or Mn2+-activated, enzyme form EII.
18
L-Glu
-
Mg2+-stimulated
18
L-Glu
-
L-Glu, biosynthetic assay, Mg2+-activated, enzyme form EII
21
L-Glu
-
Mg2+-stimulated
25
L-Glu
-
Mg2+-stimulated
0.32
L-glutamate
D51A mutant, pH 7.0, 30°C
0.37
L-glutamate
D51S mutant, pH 7.0, 30°C
0.44
L-glutamate
recombinant enzyme, coupled reactions assay, pH and temperature not specified in the publication
0.47
L-glutamate
recombinant enzyme, Malachite green assay, pH and temperature not specified in the publication
0.6
L-glutamate
pH 7.8, 30°C, isoenzyme GLN1,4
0.85
L-glutamate
D51N mutant, pH 7.0, 30°C
1 - 4
L-glutamate
pH 7.0, temperature not specified in the publication, mutant R62A
1.1
L-glutamate
-
short isoform, pH 7.2, 37°C
1.1
L-glutamate
pH 7.8, 30°C, isoenzyme GLN1,1
1.3
L-glutamate
-
long isoform, pH 7.2, 37°C
1.5
L-glutamate
wild type enzyme, pH 7.0, 30°C
1.7 - 2
L-glutamate
-
isozyme GSIII-2, pH 7.5, 37°C, glutamine synthetase activity
1.9
L-glutamate
30°C, isoenzyme OsGLN1,1
2
L-glutamate
-
mutant enzyme, pH 7.5, 37°C
3.4
L-glutamate
-
mutant E304H, 25°C, pH not specified in the publication
3.4
L-glutamate
pH 7.0, temperature not specified in the publication, mutant E304A
3.8
L-glutamate
pH 7.8, 30°C, isoenzyme GLN1,2
3.9
L-glutamate
pH 7.8, 30°C, isoenzyme GLN1,3
5.7
L-glutamate
pH not specified in the publication, 30°C, wild-type mature enzyme
7
L-glutamate
-
wild-type enzyme, pH 7.5, 37°C
7
L-glutamate
-
wild type enzyme, pH 7.5, 37°C
8.58
L-glutamate
-
isozyme GSIII-1, pH 7.5, 37°C, glutamine synthetase activity
10
L-glutamate
-
mutant E304D, 25°C, pH not specified in the publication
11.52
L-glutamate
pH not specified in the publication, 30°C, mutant mature enzyme lacking the C-terminal peptide
16
L-glutamate
D51E mutant, pH 7.0, 30°C
18
L-glutamate
-
D56E mutant enzyme, pH 7.5, 37°C
22
L-glutamate
-
chloroplast enzyme
23.5
L-glutamate
60°C, pH 7.8
26.3
L-glutamate
recombinant enzyme, pH 7.8, 37°C
27
L-glutamate
-
wild-type enzyme
27
L-glutamate
-
wild-type, 25°C, pH not specified in the publication
27
L-glutamate
pH 7.0, temperature not specified in the publication, wild-type enzyme
29
L-glutamate
-
mutant enzyme S186F
38
L-glutamate
-
D56A mutant enzyme, pH 7.5, 37°C
58
L-glutamate
pH 7.0, 60°C
59
L-glutamate
-
mutant Y303H, 25°C, pH not specified in the publication
84
L-glutamate
-
mutant G302A, 25°C, pH not specified in the publication
104
L-glutamate
-
pH 7.0, 37°C
0.00673
L-glutamine
pH 6.0, 35°C, recombinant mutant E60A/R64G
0.00888
L-glutamine
pH 6.0, 35°C, recombinant mutant E60A
0.00982
L-glutamine
pH 6.0, 35°C, recombinant mutant R64G
0.012
L-glutamine
pH 6.0, 35°C, recombinant wild-type enzyme
0.62
L-glutamine
-
isozyme GSIII-2, pH 6.0, 37°C, gamma-glutamylhydroxamate synthetase activity
1.3
L-glutamine
-
isozyme GSIII-1, pH 6.0, 37°C, gamma-glutamylhydroxamate synthetase activity
1.93
L-glutamine
-
isozyme GSI, pH 6.0, 37°C, gamma-glutamylhydroxamate synthetase activity
6.8
L-glutamine
pH 6.4, 37°C, wild-type enzyme
13
L-glutamine
-
wild-type enzyme
14
L-glutamine
-
mutant enzyme S186F
20
methylamine
-
pH 8.0, 3 mM Mn2+
100
methylamine
-
pH 8.5, 30 mM Mg2+
0.18
NH3
-
wild-type, 25°C, pH not specified in the publication
0.18
NH3
pH 7.0, temperature not specified in the publication, wild-type enzyme
0.34
NH3
pH 7.0, temperature not specified in the publication, mutant R62A
0.43
NH3
-
isozyme GSIII-2, pH 7.5, 37°C, glutamine synthetase activity
0.48
NH3
-
isozyme GSIII-1, pH 7.5, 37°C, glutamine synthetase activity
32
NH3
-
mutant E304H, 25°C, pH not specified in the publication
32
NH3
pH 7.0, temperature not specified in the publication, mutant E304A
120
NH3
-
mutant E304D, 25°C, pH not specified in the publication
0.004
NH4+
-
enzyme from strain SA0, pH 6.8
0.01
NH4+
pH 7.8, 30°C, below, isoenzyme GLN1,1
0.0125
NH4+
-
biosynthetic assay
0.013
NH4+
-
D56E mutant enzyme, pH 7.5, 37°C
0.015
NH4+
-
enzyme from strain SA0, pH 7.5
0.02
NH4+
-
D56A mutant enzyme, pH 7.5, 37°C
0.02 - 0.05
NH4+
-
isoforms GSI and GSII
0.025
NH4+
-
wild type enzyme, pH 7.5, 37°C
0.027
NH4+
30°C, isoenzyme OsGLN1,1
0.028
NH4+
-
pH 7.4, 35°C
0.042
NH4+
-
in the presence of Mg2+
0.05
NH4+
wild type enzyme, pH 7.0, 30°C
0.073
NH4+
30°C, isoenzyme OsGLN1,2
0.119
NH4+
mutant A174S of isoenzyme GLN1,4
0.12
NH4+
isoenzyme GLN1,4
0.18
NH4+
-
Mg2+-stimulated
0.19
NH4+
-
enzyme form GSIII
0.2
NH4+
-
biosynthetic assay
0.2
NH4+
-
NH4+, biosynthetic assay, Mg2+-activated, enzyme form EII
0.334
NH4+
mutant A174S of isoenzyme GLN1,3
0.4
NH4+
-
chloroplast enzyme
0.45
NH4+
mutant K49Q of isoenzyme GLN1,3
0.453
NH4+
mutant K49Q of isoenzyme GLN1,4
0.456
NH4+
mutant K49Q/A174S of isoenzyme GLN1,3
0.48
NH4+
-
biosynthetic assay, Mn2+-stimulated, enzyme form EI
0.55
NH4+
D51E mutant, pH 7.0, 30°C
0.56
NH4+
-
Mg2+-stimulated
0.56
NH4+
-
hydroxylamine, Mg2+-activated, enzyme form EII
0.56
NH4+
-
pH 8.0, 30 mM Mg2+
0.58
NH4+
pH 7.8, 30°C, below, isoenzyme GLN1,4
0.59
NH4+
-
Mg2+-stimulated
0.59
NH4+
-
pH 7.5, 3 mM MN2+
0.69
NH4+
-
Mn2+-stimulated
0.69
NH4+
-
NH4+, Mg2+-stimulated
0.71
NH4+
-
Mn2+-stimulated
0.736
NH4+
mutant K49Q/A174S of isoenzyme GLN1,4
0.77
NH4+
-
Mn2+-stimulated
0.78
NH4+
recombinant enzyme, Malachite green assay, pH and temperature not specified in the publication
0.79
NH4+
recombinant enzyme, coupled reactions assay, pH and temperature not specified in the publication
0.92
NH4+
D51N mutant, pH 7.0, 30°C
1.21
NH4+
pH 7.8, 30°C, below, isoenzyme GLN1,3
1.33
NH4+
isoenzyme GLN1,3
1.4
NH4+
-
enzyme from strain SA1, pH 7.5
2.45
NH4+
pH 7.8, 30°C, below, isoenzyme GLN1,2
5.95
NH4+
D51S mutant, pH 7.0, 30°C
12.4
NH4+
-
enzyme from strain SA1, pH 6.8
12.45
NH4+
D51A mutant, pH 7.0, 30°C
33
NH4+
-
enzyme form GSIII
additional information
hydroxylamine
the Km value of GlnA for hydroxylamine is higher when a high concentration was used (5 to 30mM), 60°C, pH 7.8
additional information
hydroxylamine
-
the Km value of GlnA for hydroxylamine is higher when a high concentration was used (5 to 30mM), 60°C, pH 7.8
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
ADP-ribosylation of glutamine synthetase could be an alternative modification to adenylylation to regulate glutamine synthetase activity
-
additional information
additional information
-
Km-values of wild-type and mutant enzymes D50A, D50E, E327A
-
additional information
additional information
-
the enzyme is modulated by a closed bicyclic covalent interconvertible cascade. It consists of two protein nucleotidylation cycles. One involves the cyclic adenylylation and deadenylylation of glutamine synthetase, the other involves the uridylylation and deuridylylation of Shapiro´s regulatory protein PII
-
additional information
additional information
-
the site of ADP-ribosylation is Arg172
-
additional information
additional information
-
enzyme activity is controlled by adenylylation
-
additional information
additional information
-
enzyme activity is controlled by adenylylation
-
additional information
additional information
-
Km for Gln and Glu increases after adenylylation
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
the enzymatic rate of GS enzymes shows a hyperbolic curve typical of the enzymes that follow the Michaelis-Menten equation regarding the ATP and glutamate and a sigmoidal curve relative to the hydroxylamine concentration
-
additional information
additional information
-
the enzymatic rate of GS enzymes shows a hyperbolic curve typical of the enzymes that follow the Michaelis-Menten equation regarding the ATP and glutamate and a sigmoidal curve relative to the hydroxylamine concentration
-
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0.033
(2S)-2-amino-4-(methylsulfonyl)butanoic acid
Mycobacterium tuberculosis
pH 7.5, 22°C
0.056 - 0.058
(2S,5R)-2,6-diamino-5-hydroxyhexanoic acid
Mycobacterium tuberculosis
dependent on the solvent, pH 7.5, 22°C
0.447
([[(2,4-dichlorophenyl)methyl]amino]methylene)bis(phosphonic acid)
Mycobacterium tuberculosis
pH 7.5, 22°C
0.331
([[(2,5-dichlorophenyl)methyl]amino]methylene)bis(phosphonic acid)
Mycobacterium tuberculosis
pH 7.5, 22°C
0.0025
1-[(3,4-dichlorophenyl)methyl]-3,7-dimethyl-8-(morpholin-4-yl)-3,7-dihydro-1H-purine-2,6-dione
Mycobacterium tuberculosis
pH and temperature not specified in the publication
0.0025
1-[(3,4-dichlorophenyl)methyl]-3,7-dimethyl-8-morpholin-4-yl-purine-2,6-dione
Mycobacterium tuberculosis
-
0.017
1-[(3,4-dichlorophenyl)methyl]-8-[(2-methoxyethyl)amino]-3,7-dimethyl-3,7-dihydro-1H-purine-2,6-dione
Mycobacterium tuberculosis
pH and temperature not specified in the publication
0.01
2-(3-aminophenyl)-6-bromo-N-cyclopentylimidazo[1,2-a]pyridin-3-amine
Mycobacterium tuberculosis
-
-
0.026
2-amino-4-(hydroxyamino)butanoic acid
Mycobacterium tuberculosis
pH 7.5, 22°C
0.025
2-tert-butyl-4-(6-methoxynaphthalen-2-yl)-5-phenyl-1H-imidazole
Mycobacterium tuberculosis
-
above, pH and temperature not specified in the publication
0.025
2-[2-tert-butyl-4-(6-methoxynaphthalen-2-yl)-1H-imidazol-5-yl]pyrimidine
Mycobacterium tuberculosis
-
above, pH and temperature not specified in the publication
0.0063
2-[4-[6-bromo-3-(butylamino)imidazo[1,2-a]pyridin-2-yl]phenoxy]acetamide
Mycobacterium tuberculosis
pH and temperature not specified in the publication
0.003
2-[4-[6-bromo-3-(butylamino)imidazo[1,2-a]pyridin-2-yl]phenoxy]ethan-1-ol
Mycobacterium tuberculosis
pH and temperature not specified in the publication
0.0083
2-[[4-[6-bromo-3-(butylamino)imidazo[1,2-a]pyridin-2-yl]phenyl](methyl)amino]ethan-1-ol
Mycobacterium tuberculosis
pH and temperature not specified in the publication
0.053
3,4-dichlorophenylethylidene-1-hydroxy-1,1-bisphosphonic acid
Mycobacterium tuberculosis
pH 7.5, 22°C
0.082
3,5-difluorophenylaminoethylidenebisphosphonic acid
Mycobacterium tuberculosis
pH 7.5, 22°C
0.00002
3-[2-tert-butyl-5-(pyridin-4-yl)-1H-imidazol-4-yl]quinoline
Mycobacterium tuberculosis
-
pH and temperature not specified in the publication
0.025
3-[4-(6-methoxynaphthalen-2-yl)-5-(pyridin-4-yl)-1H-imidazol-2-yl]phenol
Mycobacterium tuberculosis
-
above, pH and temperature not specified in the publication
0.0006
3-[6-bromo-3-(butylamino)imidazo[1,2-a]pyridin-2-yl]benzoic acid
Mycobacterium tuberculosis
pH and temperature not specified in the publication
0.0014
3-[6-bromo-3-(butylamino)imidazo[1,2-a]pyridin-2-yl]phenol
Mycobacterium tuberculosis
pH and temperature not specified in the publication
0.00038
3-[6-bromo-3-(cyclopentylamino)imidazo[1,2-a]pyridin-2-yl]benzoic acid
0.0033
3-[6-bromo-3-(cyclopentylamino)imidazo[1,2-a]pyridin-2-yl]phenol
0.125
4-methylphenylethylidene-1-hydroxy-1,1-bisphosphonic acid
Mycobacterium tuberculosis
pH 7.5, 22°C
0.0022
4-[2-ethyl-4-(6-methoxynaphthalen-2-yl)-1H-imidazol-5-yl]pyridine
Mycobacterium tuberculosis
-
pH and temperature not specified in the publication
0.0012
4-[2-tert-butyl-4-(6-methoxynaphthalen-2-yl)-1H-imidazol-5-yl]-2-fluoropyridine
Mycobacterium tuberculosis
-
pH and temperature not specified in the publication
0.000049
4-[2-tert-butyl-4-(6-methoxynaphthalen-2-yl)-1H-imidazol-5-yl]pyridin-2-amine
Mycobacterium tuberculosis
pH and temperature not specified in the publication
0.0031
4-[2-tert-butyl-4-(6-methoxynaphthalen-2-yl)-1H-imidazol-5-yl]pyridine
0.025
4-[4-(6-methoxynaphthalen-2-yl)-1H-imidazol-5-yl]pyridine
Mycobacterium tuberculosis
-
above, pH and temperature not specified in the publication
0.025
4-[4-(6-methoxynaphthalen-2-yl)-2-(1H-pyrrol-2-yl)-1H-imidazol-5-yl]pyridine
Mycobacterium tuberculosis
-
above, pH and temperature not specified in the publication
0.025
4-[4-(6-methoxynaphthalen-2-yl)-2-(2-phenylpropan-2-yl)-1H-imidazol-5-yl]pyridine
Mycobacterium tuberculosis
-
above, pH and temperature not specified in the publication
0.025
4-[4-(6-methoxynaphthalen-2-yl)-2-methyl-1H-imidazol-5-yl]pyridine
Mycobacterium tuberculosis
-
above, pH and temperature not specified in the publication
0.025
4-[4-(6-methoxynaphthalen-2-yl)-2-phenyl-1H-imidazol-5-yl]pyridine
Mycobacterium tuberculosis
-
above, pH and temperature not specified in the publication
0.000219
5-(2-methoxyethyl)-9-phenyl-5,10-dihydro-4H-imidazo[1,2-a]indeno[1,2-e]pyrazin-4-one
Mycobacterium tuberculosis
pH and temperature not specified in the publication
0.000066
5-(3-methylbutyl)-9-(pyridin-3-yl)-5,10-dihydro-4H-imidazo[1,2-a]indeno[1,2-e]pyrazin-4-one
Mycobacterium tuberculosis
pH and temperature not specified in the publication
0.000007
5-(but-3-en-1-yl)-9-(pyridin-3-yl)-5,10-dihydro-4H-imidazo[1,2-a]indeno[1,2-e]pyrazin-4-one
Mycobacterium tuberculosis
pH and temperature not specified in the publication
0.000663
5-benzyl-9-phenyl-5,10-dihydro-4H-imidazo[1,2-a]indeno[1,2-e]pyrazin-4-one
Mycobacterium tuberculosis
pH and temperature not specified in the publication
0.000456
5-cyclopropyl-9-(pyridin-2-yl)-5,10-dihydro-4H-imidazo[1,2-a]indeno[1,2-e]pyrazin-4-one
Mycobacterium tuberculosis
pH and temperature not specified in the publication
0.00017
5-methyl-9-phenyl-5,10-dihydro-4H-imidazo[1,2-a]indeno[1,2-e]pyrazin-4-one
Mycobacterium tuberculosis
pH and temperature not specified in the publication
0.025
5-[2-tert-butyl-4-(6-methoxynaphthalen-2-yl)-1H-imidazol-5-yl]pyrimidine
Mycobacterium tuberculosis
-
above, pH and temperature not specified in the publication
0.000084
5-[3-(dimethylamino)propyl]-9-(3-methoxyphenyl)-5,10-dihydro-4H-imidazo[1,2-a]indeno[1,2-e]pyrazin-4-one
Mycobacterium tuberculosis
pH and temperature not specified in the publication
0.000857
5-[3-(dimethylamino)propyl]-9-(pyridin-2-yl)-5,10-dihydro-4H-imidazo[1,2-a]indeno[1,2-e]pyrazin-4-one
Mycobacterium tuberculosis
pH and temperature not specified in the publication
0.000131
5-[3-(dimethylamino)propyl]-9-(pyridin-3-yl)-5,10-dihydro-4H-imidazo[1,2-a]indeno[1,2-e]pyrazin-4-one
Mycobacterium tuberculosis
pH and temperature not specified in the publication
0.0019
5-[6-bromo-3-(butylamino)imidazo[1,2-a]pyridin-2-yl]-2-methoxyphenol
Mycobacterium tuberculosis
pH and temperature not specified in the publication
0.0025 - 0.0088
5-[6-bromo-3-(cyclopentylamino)imidazo[1,2-a]pyridin-2-yl]-2-methoxyphenol
0.0048
5-[6-iodo-3-(cyclopentylamino)imidazo[1,2-a]pyridin-2-yl]-2-methoxyphenol
Mycobacterium tuberculosis
-
-
0.0058
6-bromo-N-butyl-2-[4-[2-(dimethylamino)ethoxy]phenyl]imidazo[1,2-a]pyridin-3-amine
Mycobacterium tuberculosis
pH and temperature not specified in the publication
0.00061
9-(3-chlorophenyl)-5,10-dihydro-4H-imidazo[1,2-a]indeno[1,2-e]pyrazin-4-one
Mycobacterium tuberculosis
pH and temperature not specified in the publication
0.000051
9-(3-methoxyphenyl)-5,10-dihydro-4H-imidazo[1,2-a]indeno[1,2-e]pyrazin-4-one
Mycobacterium tuberculosis
pH and temperature not specified in the publication
0.000031
9-(pyridin-3-yl)-5,10-dihydro-4H-imidazo[1,2-a]indeno[1,2-e]pyrazin-4-one
Mycobacterium tuberculosis
pH and temperature not specified in the publication
0.007
9-(quinolin-5-yl)-5,10-dihydro-4H-imidazo[1,2-a]indeno[1,2-e]pyrazin-4-one
Mycobacterium tuberculosis
pH and temperature not specified in the publication
0.00003
9-bromo-5,10-dihydro-4H-imidazo[1,2-a]indeno[1,2-e]pyrazin-4-one
Mycobacterium tuberculosis
pH and temperature not specified in the publication
0.000031
9-phenyl-5,10-dihydro-4H-imidazo[1,2-a]indeno[1,2-e]pyrazin-4-one
Mycobacterium tuberculosis
pH and temperature not specified in the publication
0.000333
9-phenyl-5-(prop-2-en-1-yl)-5,10-dihydro-4H-imidazo[1,2-a]indeno[1,2-e]pyrazin-4-one
Mycobacterium tuberculosis
pH and temperature not specified in the publication
0.244
benzylethylidene-1-hydroxy-1,1-bisphosphonic acid
Mycobacterium tuberculosis
pH 7.5, 22°C
3
L-methionine S-sulfoximine
Mycobacterium tuberculosis
-
IC50: 3 mM
0.081
L-methionine sulfoximine
Mycobacterium tuberculosis
pH 7.5, 22°C
0.051
L-methionine-(S)-sulfoximine
Mycobacterium tuberculosis
pH 7.5, 22°C
0.1 - 26
L-methionine-S-sulfoximine
0.0207 - 0.051
methionine sulfoximine
0.231
N-(4-isopropylphenyl)aminomethylenebisphosphonic acid
Mycobacterium tuberculosis
pH 7.5, 22°C
0.249
N-(4-methylphenyl)aminoethalidenebisphosphonic acid
Mycobacterium tuberculosis
pH 7.5, 22°C
0.0021
N-(4-oxo-5,10-dihydro-4H-imidazo[1,2-a]indeno[1,2-e]pyrazin-9-yl)acetamide
Mycobacterium tuberculosis
pH and temperature not specified in the publication
0.174
N-phenylaminoethalidenebisphosphonic acid
Mycobacterium tuberculosis
pH 7.5, 22°C
0.246
N-phenylaminomethylenebisphosphonic acid
Mycobacterium tuberculosis
pH 7.5, 22°C
0.2
Ni2+
Rattus norvegicus
-
pH 6.2, 37°C
0.221
phenylethylidene-1-hydroxy-1,1-bisphosphonic acid
Mycobacterium tuberculosis
pH 7.5, 22°C
0.348
phenylmethylidene-1-hydroxy-1,1-bisphosphonic acid
Mycobacterium tuberculosis
pH 7.5, 22°C
0.0019 - 0.076
Phosphinothricin
0.186
[(2-chloro-3-methylphenyl)(hydroxy)methylene]bis(phosphonic acid)
Mycobacterium tuberculosis
pH 7.5, 22°C
0.358
[(2-chloroanilino)methylene]bis(phosphonic acid)
Mycobacterium tuberculosis
pH 7.5, 22°C
0.317
[(3,4-dichloroanilino)methylene]bis(phosphonic acid)
Mycobacterium tuberculosis
pH 7.5, 22°C
0.228
[(3,5-dichloroanilino)methylene]bis(phosphonic acid)
Mycobacterium tuberculosis
pH 7.5, 22°C
0.269
[(3,5-difluoroanilino)methylene]bis(phosphonic acid)
Mycobacterium tuberculosis
pH 7.5, 22°C
0.227
[(3,5-dimethylanilino)methylene]bis(phosphonic acid)
Mycobacterium tuberculosis
pH 7.5, 22°C
0.345
[(3,5-dimethylphenyl)(hydroxy)methylene]bis(phosphonic acid)
Mycobacterium tuberculosis
pH 7.5, 22°C
0.273
[(3-carbamoylanilino)methylene]bis(phosphonic acid)
Mycobacterium tuberculosis
pH 7.5, 22°C
0.24
[(3-chloroanilino)methylene]bis(phosphonic acid)
Mycobacterium tuberculosis
pH 7.5, 22°C
0.25
[(4-benzylanilino)methylene]bis(phosphonic acid)
Mycobacterium tuberculosis
pH 7.5, 22°C
0.363
[(4-benzylphenyl)(hydroxy)methylene]bis(phosphonic acid)
Mycobacterium tuberculosis
pH 7.5, 22°C
0.375
[(4-chloroanilino)methylene]bis(phosphonic acid)
Mycobacterium tuberculosis
pH 7.5, 22°C
0.525
[(4-methylanilino)methylene]bis(phosphonic acid)
Mycobacterium tuberculosis
pH 7.5, 22°C
0.178
[2-(2,3-dichlorophenyl)-1-hydroxyethane-1,1-diyl]bis(phosphonic acid)
Mycobacterium tuberculosis
pH 7.5, 22°C
0.18
[2-(2,6-dichloroanilino)ethane-1,1-diyl]bis(phosphonic acid)
Mycobacterium tuberculosis
pH 7.5, 22°C
0.194
[2-(2,6-dichlorophenyl)-1-hydroxyethane-1,1-diyl]bis(phosphonic acid)
Mycobacterium tuberculosis
pH 7.5, 22°C
0.082
[2-(3,5-dichloroanilino)ethane-1,1-diyl]bis(phosphonic acid)
Mycobacterium tuberculosis
pH 7.5, 22°C
0.45
[2-(3,5-dimethylphenyl)-1-hydroxyethane-1,1-diyl]bis(phosphonic acid)
Mycobacterium tuberculosis
pH 7.5, 22°C
0.286
[2-(4-benzylanilino)ethane-1,1-diyl]bis(phosphonic acid)
Mycobacterium tuberculosis
pH 7.5, 22°C
0.13
[2-(4-chlorophenyl)-1-hydroxyethane-1,1-diyl]bis(phosphonic acid)
Mycobacterium tuberculosis
pH 7.5, 22°C
0.294
[2-[(5,6,7,8-tetrahydronaphthalen-1-yl)amino]ethane-1,1-diyl]bis(phosphonic acid)
Mycobacterium tuberculosis
pH 7.5, 22°C
0.168
[2-[3,5-bis(trifluoromethyl)anilino]ethane-1,1-diyl]bis(phosphonic acid)
Mycobacterium tuberculosis
pH 7.5, 22°C
0.0132
[3-[6-bromo-3-(cyclopentylamino)imidazo[1,2-a]pyridin-2-yl]phenyl]methanol
Mycobacterium tuberculosis
-
-
0.0016
[4-[6-bromo-3-(butylamino)imidazo[1,2-a]pyridin-2-yl]phenoxy]acetic acid
Mycobacterium tuberculosis
pH and temperature not specified in the publication
0.0128
[[(2,3-dichlorophenyl)amino]methanediyl]bis(phosphonic acid)
Zea mays
-
0.286
[[(2,3-dihydro-1H-inden-5-yl)amino]methylene]bis(phosphonic acid)
Mycobacterium tuberculosis
pH 7.5, 22°C
0.0212
[[(2,4-dichlorophenyl)amino]methanediyl]bis(phosphonic acid)
Zea mays
-
0.015
[[(2,6-dichlorophenyl)amino]methanediyl]bis(phosphonic acid)
Zea mays
-
0.0076
[[(3,5-dichlorophenyl)amino]methanediyl]bis(phosphonic acid)
Zea mays
-
0.021
[[(4-chlorophenyl)amino]methanediyl]bis(phosphonic acid)
Zea mays
-
0.278
[[(5,6,7,8-tetrahydronaphthalen-2-yl)amino]methylene]bis(phosphonic acid)
Mycobacterium tuberculosis
pH 7.5, 22°C
0.256
[[3-(trifluoromethyl)anilino]methylene]bis(phosphonic acid)
Mycobacterium tuberculosis
pH 7.5, 22°C
additional information
additional information
-
0.00038
3-[6-bromo-3-(cyclopentylamino)imidazo[1,2-a]pyridin-2-yl]benzoic acid
Mycobacterium tuberculosis
-
-
0.00038
3-[6-bromo-3-(cyclopentylamino)imidazo[1,2-a]pyridin-2-yl]benzoic acid
Mycobacterium tuberculosis
pH and temperature not specified in the publication
0.0033
3-[6-bromo-3-(cyclopentylamino)imidazo[1,2-a]pyridin-2-yl]phenol
Mycobacterium tuberculosis
-
-
0.0033
3-[6-bromo-3-(cyclopentylamino)imidazo[1,2-a]pyridin-2-yl]phenol
Mycobacterium tuberculosis
pH and temperature not specified in the publication
0.0031
4-[2-tert-butyl-4-(6-methoxynaphthalen-2-yl)-1H-imidazol-5-yl]pyridine
Mycobacterium tuberculosis
-
pH and temperature not specified in the publication
0.0031
4-[2-tert-butyl-4-(6-methoxynaphthalen-2-yl)-1H-imidazol-5-yl]pyridine
Mycobacterium tuberculosis
pH and temperature not specified in the publication
0.0025
5-[6-bromo-3-(cyclopentylamino)imidazo[1,2-a]pyridin-2-yl]-2-methoxyphenol
Mycobacterium tuberculosis
pH and temperature not specified in the publication
0.0088
5-[6-bromo-3-(cyclopentylamino)imidazo[1,2-a]pyridin-2-yl]-2-methoxyphenol
Mycobacterium tuberculosis
-
-
0.2
AMP
Bacillus subtilis
-
mutant P306A, 25°C, pH not specified in the publication
0.5
AMP
Bacillus subtilis
-
wild-type, 25°C, pH not specified in the publication
1
AMP
Bacillus subtilis
-
mutant Y303H, 25°C, pH not specified in the publication
1.3
AMP
Bacillus subtilis
-
mutant Y303A, 25°C, pH not specified in the publication
1.4
AMP
Bacillus subtilis
-
mutant V300A, 25°C, pH not specified in the publication
1.5
AMP
Bacillus subtilis
-
mutant Y303L, 25°C, pH not specified in the publication
1.7
AMP
Bacillus subtilis
-
mutant E304D, 25°C, pH not specified in the publication
1.7
AMP
Bacillus subtilis
-
mutant G302A, 25°C, pH not specified in the publication
2.1
AMP
Bacillus subtilis
-
mutant A305G, 25°C, pH not specified in the publication
30
AMP
Bacillus subtilis
-
mutant E304A, 25°C, pH not specified in the publication
31
glycine
Bacillus subtilis
-
wild-type, 25°C, pH not specified in the publication
350
glycine
Bacillus subtilis
-
mutant A305G, 25°C, pH not specified in the publication
1.5
L-glutamine
Bacillus subtilis
-
mutant P306A, 25°C, pH not specified in the publication
2.4
L-glutamine
Bacillus subtilis
-
wild-type, 25°C, pH not specified in the publication
4.1
L-glutamine
Bacillus subtilis
-
mutant Y303H, 25°C, pH not specified in the publication
7
L-glutamine
Bacillus subtilis
-
mutant V300A, 25°C, pH not specified in the publication
11
L-glutamine
Bacillus subtilis
-
mutant G302A, 25°C, pH not specified in the publication
13
L-glutamine
Bacillus subtilis
-
mutant Y303A, 25°C, pH not specified in the publication
19
L-glutamine
Bacillus subtilis
-
mutant Y303L, 25°C, pH not specified in the publication
79
L-glutamine
Bacillus subtilis
-
mutant E304D, 25°C, pH not specified in the publication
140
L-glutamine
Bacillus subtilis
-
mutant A305G, 25°C, pH not specified in the publication
140
L-glutamine
Bacillus subtilis
-
mutant E304A, 25°C, pH not specified in the publication
0.1
L-methionine-S-sulfoximine
Bacillus subtilis
-
mutant Y303H, 25°C, pH not specified in the publication
0.1
L-methionine-S-sulfoximine
Bacillus subtilis
-
mutant Y303L, 25°C, pH not specified in the publication
0.104
L-methionine-S-sulfoximine
Mycobacterium tuberculosis
pH 7.5, 22°C, recombinant enzyme
0.12
L-methionine-S-sulfoximine
Bacillus subtilis
-
mutant V300A, 25°C, pH not specified in the publication
0.13
L-methionine-S-sulfoximine
Bacillus subtilis
-
wild-type, 25°C, pH not specified in the publication
0.25
L-methionine-S-sulfoximine
Bacillus subtilis
-
mutant P306A, 25°C, pH not specified in the publication
0.28
L-methionine-S-sulfoximine
Bacillus subtilis
-
mutant G302A, 25°C, pH not specified in the publication
0.61
L-methionine-S-sulfoximine
Bacillus subtilis
-
mutant Y303A, 25°C, pH not specified in the publication
2.7
L-methionine-S-sulfoximine
Bacillus subtilis
-
mutant A305G, 25°C, pH not specified in the publication
20
L-methionine-S-sulfoximine
Bacillus subtilis
-
mutant E304D, 25°C, pH not specified in the publication
26
L-methionine-S-sulfoximine
Bacillus subtilis
-
mutant E304A, 25°C, pH not specified in the publication
0.0207
methionine sulfoximine
Trypanosoma cruzi
recombinant enzyme, pH and temperature not specified in the publication
0.051
methionine sulfoximine
Mycobacterium tuberculosis
pH and temperature not specified in the publication
0.0019
Phosphinothricin
Mycobacterium tuberculosis
pH 7.5, 22°C
0.076
Phosphinothricin
Mycobacterium tuberculosis
pH 7.5, 22°C
additional information
additional information
Mycobacterium tuberculosis
IC50 values of the compounds versus Mycobacterium tuberculosis cells and human Hep-G2 cells
-
additional information
additional information
Mycobacterium tuberculosis
-
IC50 values of the compounds versus Mycobacterium tuberculosis cells and human Hep-G2 cells
-
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-
-
brenda
-
of root nodules
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
no significant changes in the enzyme activity between morphine-treated and control samples
brenda
-
-
brenda
-
-
brenda
-
-
brenda
in the nonblastemal regions of regenerating fragments and in intact worms
brenda
-
brenda
-
-
brenda
-
anterior corpus striatum
brenda
-
astrocyte-like cells
brenda
-
-
brenda
-
brenda
the enzyme persist in the epidermal cells during the formation and elongation of the blastema
brenda
-
-
brenda
of buccal and pharyngeal cavities
brenda
-
brenda
-
brenda
-
tissue distribution, immunohistochemic analysis
brenda
association with
brenda
-
fetal
brenda
-
enzyme form Gln1-3, and enzyme form Gln1-5 at a low level
brenda
-
-
brenda
-
-
brenda
in the nonblastemal regions of regenerating fragments and in intact worms
brenda
Azolla sp.
-
-
brenda
-
brenda
-
brenda
-
brenda
in 28-day adult worms
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
high expression level
brenda
-
astrocyte-like cells
brenda
-
osteoblast-like cells
brenda
-
-
brenda
in the nonblastemal regions of regenerating fragments and in intact worms
brenda
-
-
brenda
-
-
brenda
in the nonblastemal regions of regenerating fragments and in intact worms
brenda
-
brenda
pancreatic endocrine tumor, solid and pseudopapillary neoplasms, the enzyme is overexpressed by 3-13fold in pancreatic tumors compared to healthy tissue, overview
brenda
in 28-day adult worms
brenda
-
brenda
-
brenda
-
level of expression of glutamine synthetase in equine placenta and pregnant and non-pregnant horns, overview
brenda
-
brenda
-
a rat brain-derived type-2 astrocyte cell line
brenda
-
loss of glutamine synthetase immunoreactivity from the retina in canine primary glaucoma, immunohistochemic analysis, overview
brenda
-
-
brenda
-
post-acrosomal region of the perinuclear theca, a major cytoskeletal component of the sperm head
brenda
in the nonblastemal regions of regenerating fragments and in intact worms
brenda
-
-
brenda
-
isoenzyme GS1
brenda
-
brenda
-
-
brenda
-
brenda
-
no significant changes in the enzyme activity between morphine-treated and control samples
brenda
-
moderate expression level
brenda
-
level of expression of glutamine synthetase in equine placenta and pregnant and non-pregnant horns, enzyme abundance is higher in pregnant area than in non-pregnant horn, overview
brenda
-
low expression level
brenda
-
brenda
-
-
brenda
-
higher to moderate expression level
brenda
-
-
brenda
-
brenda
-
-
-
brenda
expression levels are maximal in the amastigote stage of the life cycle, when amino acids are preferably consumed, and NH4+ production is predictable
brenda
-
expression levels are maximal in the amastigote stage of the life cycle, when amino acids are preferably consumed, and NH4+ production is predictable
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
primary cell culture
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
primary
brenda
-
astrocyte-specific glutamine synthetase
brenda
-
cultured cortical astrocytes maintained with endothelins show an almost complete loss of glutamine synthetase
brenda
-
-
brenda
-
-
brenda
-
brenda
-
short and long isoform
brenda
-
-
brenda
-
brenda
in prostomium, aterior end ventral nerve cord
brenda
-
glutamine synthetase transcripts of liver and brain cells are identical, no difference in the amino acid sequence of the protein. The N-terminus of glutamine synthetase, which constitutes a weak mitochondrial targeting signal, is sufficient to direct a chimeric protein to the mitochondria in hepatocytes and to the cytoplasm in astrocytes
brenda
-
-
brenda
-
neocortex
brenda
-
-
brenda
-
glutamine synthetase activity is relatively low in all adult tissues examined, except brain
brenda
-
-
brenda
-
-
brenda
-
cerebral cortex
brenda
-
located mainly in astrocytes
brenda
-
no significant changes in the enzyme activity between morphine-treated and control samples
brenda
-
-
brenda
-
a much larger amount of GlnA1 is produced than is necessary for normal growth by the organism and a substantial proportion of this is found in the extracellular medium of cell cultures
brenda
-
a much larger amount of GlnA1 is produced than is necessary for normal growth by the organism and a substantial proportion of this is found in the extracellular medium of cell cultures
-
brenda
-
leaf protoplast derived suspension culture
brenda
-
moderate expression level
brenda
-
-
brenda
-
brenda
-
during post-germinative growth, expression of GS2 increases and expression of GS1b decreases in cotyledons but not in the embryo axis
brenda
-
during post-germinative growth, expression of GS2 increases and expression of GS1b decreases in cotyledons but not in the embryo axis
brenda
-
-
brenda
in the nonblastemal regions of regenerating fragments and in intact worms
brenda
OsGLN1,1, under nitrogen-limited condition
brenda
OsGLN1,2, under nitrogen-sufficient condition
brenda
-
brenda
-
-
-
brenda
OsGLN1,1, under nitrogen-limited condition
brenda
OsGLN1,2, under nitrogen-sufficient condition
brenda
-
-
brenda
-
GS2 is only detected in green fruits, not detected in red, mature fruits
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
quantitative analysis of enzyme content at different epileptic stages compared to control rats, overview
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
moderate expression level
brenda
-
-
brenda
-
-
brenda
-
brenda
-
the enzyme expression pattern is completely different form the healthy cell pattern and appears diffuse and not map-like
brenda
-
-
brenda
-
-
brenda
-
brenda
-
-
brenda
-
-
brenda
glutamine synthetase protein is preferentially expressed in hepatocytes adjacent to oxygen-supplying capillaries and in previously CPS-positive hepatocytes. No shift towards a periportal or pericentral phenotype, overview
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
quantitative analysis of enzyme content at different epileptic stages compared to control rats, overview
brenda
-
no significant changes in the enzyme activity between morphine-treated and control samples
brenda
-
brenda
-
high expression level
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
brenda
isoenzyme GLN1,1
brenda
isoenzyme GLN1,2
brenda
isoenzyme GLN1,3
brenda
rosette leaves
brenda
flag and foliar leaves, isozyme GS2 expression levels in response to nitrate and ammonium levels, overview
brenda
expression of GFP driven by the Gln-1;2 promoter occurs in both developed and developing new leaves of plants in the vegetative growth stage. Bright GFP signals are detected in mesophyll cells within the margins of developed leaves. Fluorescence is also recorded in the cells of vascular bundles along the veins in developed leaves. In the developing new leaves, fluorescence is weak and signals are confined to the trichomes
brenda
-
in mesophyll cell almost all glutamine synthetase is present in chloroplasts. In hair cells, glutamine synthetase is observed both in chloroplasts and in cytoplasm
brenda
-
of seedling
brenda
-
isoenzyme GS1
brenda
-
isoenzyme GS2
brenda
specific expression
brenda
-
brenda
-
-
brenda
isozyme GS2 expression levels in response to nitrate and ammonium levels, overview
brenda
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
plastidic enzyme form is localized only in the stroma matrix of chloroplasts and plastids. Cytosolic glutamine synthetase is preferentially localized in the vascular tissue
brenda
-
brenda
-
brenda
-
brenda
-
-
brenda
-
glutamine synthetase activity is higher in the leaf than in the root, activity is higher in ammonium-fed plants than in nitrate-fed plants
brenda
-
-
brenda
-
-
brenda
-
decrease of GS2 during leaf senescence
brenda
-
increase of GS1 during leaf senescence, isoenzyme GS1
brenda
-
-
brenda
-
glutamine synthetase activity is higher in the leaf than in the root, activity is higher in ammonium-fed plants than in nitrate-fed plants
brenda
-
-
brenda
-
brenda
-
in mature flag leaves, large amounts of isoenzyme GS1 are detected in the connections between the mestome sheath cells and the vascular cells. Parallel to leaf senescence, an increase of a GS1 polypeptide (GS1b) is detected in the mesophyll cytosol of senescing leaves, while the content of another polypeptide (GS1a) in the phloem companion cells remains practically constant in both leaves and stem
brenda
-
brenda
bundle sheath and mesophyll cells, expression analysis of isozyme GS1, overview
brenda
bundle sheath and mesophyll cells, expression analysis of isozyme GS2, overview
brenda
-
GS activity is analyzed dependent on different leaf developmental stages, with or without Mg2+ starvation, overview
brenda
-
high activity at birth, increases in postnatal phase
brenda
-
-
brenda
-
brenda
-
short and long isoform
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
brenda
-
high expression level
brenda
-
higher to moderate expression level
brenda
-
-
brenda
-
activity is increased in liver during starvation
brenda
-
glutamine synthetase transcripts of liver and brain cells are identical, no difference in the amino acid sequence of the protein. The N-terminus of glutamine synthetase, which constitutes a weak mitochondrial targeting signal, is sufficient to direct a chimeric protein to the mitochondria in hepatocytes and to the cytoplasm in astrocytes
brenda
-
-
brenda
-
the cytosolic enzyme is localized in large areas, anastomosed in a map-like pattern, often surrounding hepatic veins, whereas GS is not expressed in hepatocytes close to fibrotic bands containing arteries and ductules
brenda
-
-
brenda
-
the four genes coding for glutamine synthetase (Onmy-GS01, Onmy-GS02, Onmy-GS03 and Onmy-GS04) are expressed during early development, but only Onmy-GS01 and GS02 are expressed at appreciable levels in adult liver
brenda
-
-
brenda
-
brenda
-
-
brenda
liver enzyme is targeted to mitochondria. Two different glutamine synthetase transcripts are generated by tissue-specific alternative splicing. The liver transcript contains an alternative exon that is not present in the neural one. This exon leads to acquisition of an upstream in-frame start codon and formation of a mitochondrial targeting signal
brenda
dynamic expression pattern of the enzyme in hepatocytes of different zones of the liver lobule, overview
brenda
-
moderate expression level
brenda
-
-
brenda
-
activity in breast muscle is low when compared to leg muscle
brenda
-
activity in breast muscle is low when compared to leg muscle, starvation causes no change in enzyme activity
brenda
-
-
brenda
-
-
brenda
-
brenda
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
primary derived from bone marrow
brenda
-
low expression level
brenda
-
brenda
-
brenda
-
-
-
brenda
-
brenda
-
brenda
isoenzyme GLN1,1 accumulates in the surface layers of root during nitrogen limitation
brenda
-
brenda
-
-
brenda
-
-
brenda
-
enzyme form Gln1-3, and enzyme form Gln1-5 at a low level
brenda
-
brenda
-
brenda
-
brenda
OsGLN1,1 is expressed in epidermis and exodermis under nitrogen-limited condition. Within the central cylinder of the elongating zone the enzyme is induced by ammonium
brenda
OsGLN1,2 is expressed in epidermis and exodermis under nitrogen-sufficient condition. Within the central cylinder of the elongating zone the enzyme is induced by ammonium
brenda
OsGS1;2 gene is mainly expressed in surface cells of roots
brenda
-
brenda
-
glutamine synthetase activity is higher in the leaf than in the root, activity is higher in ammonium-fed plants than in nitrate-fed plants, low activity in the dark
brenda
-
-
brenda
-
-
brenda
-
isoenzyme GS1
brenda
-
glutamine synthetase activity is higher in the leaf than in the root, activity is higher in ammonium-fed plants than in nitrate-fed plants, no relevant activity in the dark
brenda
-
brenda
-
-
brenda
-
brenda
-
-
brenda
-
brenda
-
-
brenda
-
-
brenda
-
isoenzyme GS1b (EC 6.3.1.2) in concert with NADH-dependent GOGAT (EC 1.4.1.14) constitute the major route of assimilation of ammonium derived from reserve mobilization and glutamic acid/glutamine synthesis in germinating Medicago truncatula seeds
brenda
excusively expressed in developing seeds
brenda
-
-
brenda
Sorghum sp.
-
-
brenda
-
leaf
brenda
-
brenda
-
brenda
germinating
brenda
-
-
brenda
-
brenda
-
brenda
-
of light-grown seedlings
brenda
-
-
brenda
-
of seedlings
brenda
-
inverse relationship between glutamine synthetase expression and intramuscular glutamine concentration in the horse
brenda
-
-
brenda
-
-
brenda
-
very low expression
brenda
-
low expression level
brenda
-
-
brenda
-
and hemicord
brenda
-
no significant changes in the enzyme activity between morphine-treated and control samples
brenda
neural enzyme is retained in the cytoplasm. Two different glutamine synthetase transcripts are generated by tissue-specific alternative splicing. The liver transcript contains an alternative exon that is not present in the neural one
brenda
-
brenda
-
enzyme form Gln1-5 at a high level
brenda
-
brenda
-
brenda
-
isoenzyme GS1
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
predominantly in interstitial cell
brenda
-
brenda
-
-
-
brenda
-
-
brenda
-
sprouting, isoenzyme GS1
brenda
additional information
-
expressed in nitrogen-starved plants, but 10fold less abundant than isoenzyme GLN1,1
brenda
additional information
expressed in nitrogen-starved plants, but 10fold less abundant than isoenzyme GLN1,1
brenda
additional information
expressed in nitrogen-starved plants, but 10fold less abundant than isoenzyme GLN1,1
brenda
additional information
expressed in nitrogen-starved plants, but 10fold less abundant than isoenzyme GLN1,1
brenda
additional information
-
Gln-1;4 isogene expression is very low
brenda
additional information
Gln-1;4 isogene expression is very low
brenda
additional information
Gln-1;4 isogene expression is very low
brenda
additional information
-
Gln-1;5 isogene expression is very low
brenda
additional information
Gln-1;5 isogene expression is very low
brenda
additional information
Gln-1;5 isogene expression is very low
brenda
additional information
-
Gln2 expression is high in shoots, but low in roots
brenda
additional information
Gln2 expression is high in shoots, but low in roots
brenda
additional information
Gln2 expression is high in shoots, but low in roots
brenda
additional information
isozyme Gln1-2 localizes to the vascular cells of roots, petals, and stamens
brenda
additional information
isozyme Gln1-2 localizes to the vascular cells of roots, petals, and stamens
brenda
additional information
isozymes Gln1-1 and Gln1-2 are expressed in different cell types in Arabidopsis thaliana
brenda
additional information
isozymes Gln1-1 and Gln1-2 are expressed in different cell types in Arabidopsis thaliana
brenda
additional information
-
nervous tissue distribution, immunohistochemic analysis, overview
brenda
additional information
-
nervous tissue distribution, immunohistochemic analysis, overview
brenda
additional information
gene gs expression is detectable at the cell layer covering a wound
brenda
additional information
-
gene gs expression is detectable at the cell layer covering a wound
brenda
additional information
-
pattern of glutamine synthetase expression, overview
brenda
additional information
expression analysis
brenda
additional information
-
the enzyme is ubiquitously expressed in human tissues
brenda
additional information
root nodule, isozyme MtGS1a
brenda
additional information
root nodule, isozyme MtGS1a
brenda
additional information
-
root nodule, isozyme MtGS1a
brenda
additional information
-
nervous tissue distribution, immunohistochemic analysis, overview
brenda
additional information
-
nervous tissue distribution, immunohistochemic analysis, overview
brenda
additional information
-
mRNA and protein contents of GS isoforms, overview
brenda
additional information
mRNA and protein contents of GS isoforms, overview
brenda
additional information
mRNA and protein contents of GS isoforms, overview
brenda
additional information
expression patterns and regulatory model of GS1 gene expression in pine
brenda
additional information
-
expression patterns and regulatory model of GS1 gene expression in pine
brenda
additional information
-
nervous tissue distribution, immunohistochemic analysis, overview
brenda
additional information
-
nervous tissue distribution, immunohistochemic analysis, overview
brenda
additional information
-
enzyme immunohistochemic analysis, overview
brenda
additional information
schistosomes are maintained in New Zealand rabbits. Quantitative real-time PCR expression analysis of enzyme in worms of different stages, overview
brenda
additional information
-
schistosomes are maintained in New Zealand rabbits. Quantitative real-time PCR expression analysis of enzyme in worms of different stages, overview
brenda
additional information
-
GS1 is the only glutamine synthase detected in nonphotosynthetic tissues and in later leaf senescing stages
brenda
additional information
mechanism underlying metabolic zonation, overview
brenda
additional information
-
mechanism underlying metabolic zonation, overview
brenda
additional information
-
nervous tissue distribution, immunohistochemic analysis, overview
brenda
additional information
GS1 mRNA is detected in all tissues, with transcripts being most abundant in glume and flag leaf tissue and least abundant in seedling leaves, detection by immunohistochemic analysis and in situ hybridization, overview
brenda
additional information
GS1 mRNA is detected in all tissues, with transcripts being most abundant in glume and flag leaf tissue and least abundant in seedling leaves, detection by immunohistochemic analysis and in situ hybridization, overview
brenda
additional information
GS1 mRNA is detected in all tissues, with transcripts being most abundant in glume and flag leaf tissue and least abundant in seedling leaves, detection by immunohistochemic analysis and in situ hybridization, overview
brenda
additional information
GS1 mRNA is detected in all tissues, with transcripts being most abundant in glume and flag leaf tissue and least abundant in seedling leaves, detection by immunohistochemic analysis and in situ hybridization, overview
brenda
additional information
GS1 mRNA is detected in all tissues, with transcripts being most abundant in glume and flag leaf tissue and least abundant in seedling leaves, detection by immunohistochemic analysis and in situ hybridization, overview
brenda
additional information
GS1 mRNA is detected in all tissues, with transcripts being most abundant in glume and flag leaf tissue and least abundant in seedling leaves, detection by immunohistochemic analysis and in situ hybridization, overview
brenda
additional information
GS1 mRNA is detected in all tissues, with transcripts being most abundant in glume and flag leaf tissue and least abundant in seedling leaves, detection by immunohistochemic analysis and in situ hybridization, overview
brenda
additional information
GS1 mRNA is detected in all tissues, with transcripts being most abundant in glume and flag leaf tissue and least abundant in seedling leaves, detection by immunohistochemic analysis and in situ hybridization, overview
brenda
additional information
GS1 mRNA is detected in all tissues, with transcripts being most abundant in glume and flag leaf tissue and least abundant in seedling leaves, detection by immunohistochemic analysis and in situ hybridization, overview
brenda
additional information
GS1 mRNA is detected in all tissues, with transcripts being most abundant in glume and flag leaf tissue and least abundant in seedling leaves, detection by immunohistochemic analysis and in situ hybridization, overview
brenda
additional information
-
GS1 mRNA is detected in all tissues, with transcripts being most abundant in glume and flag leaf tissue and least abundant in seedling leaves, detection by immunohistochemic analysis and in situ hybridization, overview
brenda
additional information
GS2 mRNA is detected in all wheat tissues examined, with the highest level in mature leaf and peduncle tissues, to a lesser extent in photosynthetic glumes and with some expression in the root, detection by immunohistochemic analysis and in situ hybridization, overview
brenda
additional information
GS2 mRNA is detected in all wheat tissues examined, with the highest level in mature leaf and peduncle tissues, to a lesser extent in photosynthetic glumes and with some expression in the root, detection by immunohistochemic analysis and in situ hybridization, overview
brenda
additional information
GS2 mRNA is detected in all wheat tissues examined, with the highest level in mature leaf and peduncle tissues, to a lesser extent in photosynthetic glumes and with some expression in the root, detection by immunohistochemic analysis and in situ hybridization, overview
brenda
additional information
GS2 mRNA is detected in all wheat tissues examined, with the highest level in mature leaf and peduncle tissues, to a lesser extent in photosynthetic glumes and with some expression in the root, detection by immunohistochemic analysis and in situ hybridization, overview
brenda
additional information
GS2 mRNA is detected in all wheat tissues examined, with the highest level in mature leaf and peduncle tissues, to a lesser extent in photosynthetic glumes and with some expression in the root, detection by immunohistochemic analysis and in situ hybridization, overview
brenda
additional information
GS2 mRNA is detected in all wheat tissues examined, with the highest level in mature leaf and peduncle tissues, to a lesser extent in photosynthetic glumes and with some expression in the root, detection by immunohistochemic analysis and in situ hybridization, overview
brenda
additional information
GS2 mRNA is detected in all wheat tissues examined, with the highest level in mature leaf and peduncle tissues, to a lesser extent in photosynthetic glumes and with some expression in the root, detection by immunohistochemic analysis and in situ hybridization, overview
brenda
additional information
GS2 mRNA is detected in all wheat tissues examined, with the highest level in mature leaf and peduncle tissues, to a lesser extent in photosynthetic glumes and with some expression in the root, detection by immunohistochemic analysis and in situ hybridization, overview
brenda
additional information
GS2 mRNA is detected in all wheat tissues examined, with the highest level in mature leaf and peduncle tissues, to a lesser extent in photosynthetic glumes and with some expression in the root, detection by immunohistochemic analysis and in situ hybridization, overview
brenda
additional information
GS2 mRNA is detected in all wheat tissues examined, with the highest level in mature leaf and peduncle tissues, to a lesser extent in photosynthetic glumes and with some expression in the root, detection by immunohistochemic analysis and in situ hybridization, overview
brenda
additional information
-
GS2 mRNA is detected in all wheat tissues examined, with the highest level in mature leaf and peduncle tissues, to a lesser extent in photosynthetic glumes and with some expression in the root, detection by immunohistochemic analysis and in situ hybridization, overview
brenda
additional information
GSr transcripts are prevalent in glume and root tissue but lower levels occur in leaf tissue especially at a young developmental stage, detection by immunohistochemic analysis and in situ hybridization, overview
brenda
additional information
GSr transcripts are prevalent in glume and root tissue but lower levels occur in leaf tissue especially at a young developmental stage, detection by immunohistochemic analysis and in situ hybridization, overview
brenda
additional information
GSr transcripts are prevalent in glume and root tissue but lower levels occur in leaf tissue especially at a young developmental stage, detection by immunohistochemic analysis and in situ hybridization, overview
brenda
additional information
GSr transcripts are prevalent in glume and root tissue but lower levels occur in leaf tissue especially at a young developmental stage, detection by immunohistochemic analysis and in situ hybridization, overview
brenda
additional information
GSr transcripts are prevalent in glume and root tissue but lower levels occur in leaf tissue especially at a young developmental stage, detection by immunohistochemic analysis and in situ hybridization, overview
brenda
additional information
GSr transcripts are prevalent in glume and root tissue but lower levels occur in leaf tissue especially at a young developmental stage, detection by immunohistochemic analysis and in situ hybridization, overview
brenda
additional information
GSr transcripts are prevalent in glume and root tissue but lower levels occur in leaf tissue especially at a young developmental stage, detection by immunohistochemic analysis and in situ hybridization, overview
brenda
additional information
GSr transcripts are prevalent in glume and root tissue but lower levels occur in leaf tissue especially at a young developmental stage, detection by immunohistochemic analysis and in situ hybridization, overview
brenda
additional information
GSr transcripts are prevalent in glume and root tissue but lower levels occur in leaf tissue especially at a young developmental stage, detection by immunohistochemic analysis and in situ hybridization, overview
brenda
additional information
GSr transcripts are prevalent in glume and root tissue but lower levels occur in leaf tissue especially at a young developmental stage, detection by immunohistochemic analysis and in situ hybridization, overview
brenda
additional information
-
GSr transcripts are prevalent in glume and root tissue but lower levels occur in leaf tissue especially at a young developmental stage, detection by immunohistochemic analysis and in situ hybridization, overview
brenda
additional information
the level of GSe mRNA is very low without prevalence for any tissue, detection by immunohistochemic analysis and in situ hybridization, overview
brenda
additional information
the level of GSe mRNA is very low without prevalence for any tissue, detection by immunohistochemic analysis and in situ hybridization, overview
brenda
additional information
the level of GSe mRNA is very low without prevalence for any tissue, detection by immunohistochemic analysis and in situ hybridization, overview
brenda
additional information
the level of GSe mRNA is very low without prevalence for any tissue, detection by immunohistochemic analysis and in situ hybridization, overview
brenda
additional information
the level of GSe mRNA is very low without prevalence for any tissue, detection by immunohistochemic analysis and in situ hybridization, overview
brenda
additional information
the level of GSe mRNA is very low without prevalence for any tissue, detection by immunohistochemic analysis and in situ hybridization, overview
brenda
additional information
the level of GSe mRNA is very low without prevalence for any tissue, detection by immunohistochemic analysis and in situ hybridization, overview
brenda
additional information
the level of GSe mRNA is very low without prevalence for any tissue, detection by immunohistochemic analysis and in situ hybridization, overview
brenda
additional information
the level of GSe mRNA is very low without prevalence for any tissue, detection by immunohistochemic analysis and in situ hybridization, overview
brenda
additional information
the level of GSe mRNA is very low without prevalence for any tissue, detection by immunohistochemic analysis and in situ hybridization, overview
brenda
additional information
-
the level of GSe mRNA is very low without prevalence for any tissue, detection by immunohistochemic analysis and in situ hybridization, overview
brenda
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drug target
since glutamine synthetase is the first metabolic enzyme involved in Trypanosoma cruzi evasion from the parasitophorous vacuole it is a potential target for designing anti-Trypanosoma cruzi drugs
drug target
-
since glutamine synthetase is the first metabolic enzyme involved in Trypanosoma cruzi evasion from the parasitophorous vacuole it is a potential target for designing anti-Trypanosoma cruzi drugs
-
evolution
glutamine synthetase (GS), a key enzyme in plant nitrogen metabolism, is encoded by a small family of highly homologous nuclear genes that produce cytosolic (GS1) and plastidic (GS2) isoforms. Compared to GS1, GS2 proteins have two extension peptides, one at the N- and the other at the C-terminus, which show a high degree of conservation among plant species
evolution
two GS isoforms are encoded in the genome of higher plants: the cytosolic Gln synthetase isoform (GS1) and the chloroplastic Gln synthetase isoform (GS2). GS2 is encoded by a single gene (Gln-2), whereas GS1 is encoded by a multigene family, suggesting a complex role of GS1 with respect to plant N assimilation
evolution
-
Unigene0016999 and Unigene0017002 belong to isozyme GSI, while Unigene0015608, Unigene0022741, and Unigene0002184 belong to isozyme GSII, and Unigene0002194 belongs to isozyme GSIII, sequence comparisons and phylogenetic tree, overview
malfunction
OsGS1;2 homozygously inserted mutants show severe reduction in active tiller number and hence panicle number at harvest. The mutants show marked reductions in contents of glutamine, glutamate, asparagine and aspartate, but an increase in free ammonium ions compared to the wild-type
malfunction
a gln1-1:gln1-2 double mutant shows impairment of seed germination and seedling establishment, phenotype, overview
malfunction
-
astrocytes enable the proliferation of GS-negative LN18 iRFP4 cells without Gln supplementation
malfunction
depletion of the enzyme in Hep-3B cells by transduction with two independent shRNAs reduces LC3-II formation. Conversely, exogenous enzyme overexpression increases autophagic activity in SK-Hep1 cells. Glutamine synthetase (GS) overexpression significantly increases sorafenib sensitivity in hepatocellular carcinoma cells
malfunction
enzyme mutants, single mutant gln1-2 and gln1-1:gln1-2 double mutant, show impairment of seed germination and seedling establishment. The negative effect of Gln1-2 deficiency, causing slower seedling development in the mutants, is associated with reduced N remobilization from the cotyledons and can be fully alleviated by exogenous N supply. Phenotypes, overview
malfunction
-
the total capacity of the enzyme-mediated ligation of free ammonium and glutamate to form glutamine in the leaves of maize plants is not impaired upon severe magnesium starvation. The total GS-mediated primary or secondary assimilation of free NH4+ is not a limiting enzymatic reaction under Mg-deficiency and thus cannot be accountable for the observed restriction of plant growth and productivity in Mg-deficient maize, phenotype, overview
metabolism
-
leaves of seedling grown in light for seven days contain about twofold higher glutamine synthetase activity than etiolated leaves. In both light and dark grown seedlings, total glutamine synthetase, isoforms GS1 and GS2 activities decline with plant age with more pronounced effect in leaves of etiolated seedlings. Isoform GS2 declines at a much faster rate than isoform GS1. Exposure of etiolated seedlings to light markedly enhances GS1 and GS2 activity, which is not affected by cycloheximide. Photosynthetic inhibitor dichlorophenyl dimethyl urea inhibits light dependent appearance of glutamine synthetase
metabolism
-
presence of only one glutathione synthetase inactivation factor, 7A, encoded by open reading frame asl2329, gifA. Following addition of ammonium, expression of gifA is derepressed, leading to the synthesis of IF7A, and consequently, glutathione synthetase is inactivated. Upon ammonium removal, the glutathione synthetase activity returns to the initial level and IF7A becomes undetectable. Anabaena glutathione synthetase is not inactivated by Synechocystis IFs. In an Anabaena strain expressing a second inactivating factor, containing the amino-terminal part of IF17 from Synechocystis fused to IF7A, glutathione synthetase inactivation is more effective than that in the wild-ype and resembles that observed in Synechocystis
metabolism
-
upon exposure to nitrogen limitation,GS activity increases significantly within 0.5 hrs and continues to increase significantly after 1 hr of nitrogen starvation to reach a final activity at 4 hrs that is approximately 2.5 fold greater than at zero hours. When an ammonium pulse is applied, GS activity decreases significantly within 1 hr of exposure to nitrogen excess
metabolism
glutamine synthetase plays essential roles in nitrogen metabolism
metabolism
glutamine synthetase is a key enzyme in plant nitrogen metabolism
metabolism
-
glutamine-starved GBM cells feed on astrocyte-derived glutamine. Only astrocytes demonstrate no net Gln consumption but rather, rapid Glu uptake, in line with the expression of excitatory amino acids transporters (EAAT) in this cell type. Under Gln starvation, Glu consumption is unaffected and paralleled by an equimolar net Gln efflux. The absence of Gln in the medium reduces intracellular Gln, but not Glu. Only 30-40% of both intracellular Glu and Gln are glucose-derived. Astrocytes maintain about 30% of the control level of intracellular Gln under Gln starvation, fitting with high enzyme expression. Astrocyte-derived Gln is the growth-supporting factor for Gln-starved glioblastoma cells
metabolism
the enzyme catalyzes the ATP-dependent synthesis of L-glutamine from glutamate and ammonia. GlnA1 is also involved in the synthesis of poly-L-glutamate/glutamine for the cell wall of pathogenic mycobacteria
metabolism
the glutamine synthetase/glutamate synthase cycle is considered as the major pathway for ammonium assimilation and regulation of nitrogen metabolism in higher plants
metabolism
-
presence of only one glutathione synthetase inactivation factor, 7A, encoded by open reading frame asl2329, gifA. Following addition of ammonium, expression of gifA is derepressed, leading to the synthesis of IF7A, and consequently, glutathione synthetase is inactivated. Upon ammonium removal, the glutathione synthetase activity returns to the initial level and IF7A becomes undetectable. Anabaena glutathione synthetase is not inactivated by Synechocystis IFs. In an Anabaena strain expressing a second inactivating factor, containing the amino-terminal part of IF17 from Synechocystis fused to IF7A, glutathione synthetase inactivation is more effective than that in the wild-ype and resembles that observed in Synechocystis
-
metabolism
-
glutamine synthetase plays essential roles in nitrogen metabolism
-
metabolism
-
the enzyme catalyzes the ATP-dependent synthesis of L-glutamine from glutamate and ammonia. GlnA1 is also involved in the synthesis of poly-L-glutamate/glutamine for the cell wall of pathogenic mycobacteria
-
physiological function
-
glutathione synthetase binds to transcription factor TnrA in its feedback-inhibited form, and also in its non-feedback-inhibited form, although less efficiently. TnrA forms either a stable soluble complex with GlnK in the absence of transmembrane ammonium transporter AmtB, or constitutively binds to glutathione synthetase in the absence of regulatuor GlnK. In vitro, the TnrA C-terminus is responsible for interactions with either glutathione synthetase or GlnK, and this region appears also to mediate proteolysis, suggesting that binding of GlnK or glutathione synthetase protects TnrA from degradation
physiological function
-
mice in which glutamine synthetase is selectively but completely eliminated from striated muscle are healthy and fertile. A 3-fold higher escape of ammonia reveals the absence of glutamine synthetase in muscle. After 20 h of fasting, glutamine synthetase-KO mice are not able to mount the 4fold increase in glutamine production across the hindquarter that is observed in control mice. Instead, muscle ammonia production is 5fold higher than in control mice. The fasting-induced metabolic changes are transient and return to fed levels at 36 h of fasting. Glucose consumption and lactate and ketone-body production are similar in glutamine synthetase-KO and control mice. Challenging glutamine synthetase-KO and control mice with intravenous ammonia in stepwise increments reveals that normal muscles can detoxify 2.5 mol ammonia/g muscle h in a muscle glutamine synthetase-dependent manner, with simultaneous accumulation of urea, whereas glutamine synthetase-KO mice respond with accumulation of glutamine and other amino acids, but not urea
physiological function
-
rice mutant lacking OsGS1-1 exhibits severe retardation of shoot growth in the presence of ammonium compared with the wild-type. Overaccumulation of free ammonium in the leaf sheath and roots of the mutant indicates the importance of OsGS1-1 for ammonium assimilation in both organs. The mutant line displays an imbalance in levels of sugars, amino acids and metabolites in the tricarboxylic acid cycle, and overaccumulation of secondary metabolites, particularly in the roots under a continuous supply of ammonium. Presence of mutant-specific networks between tryptamine andother primary metabolites in the roots
physiological function
-
study on glnA-1 mutant that produces reduced levels of glutamine synthetase. The mutant is able to grow in enriched 7H9 medium without glutamine supplementation.The glnA-1 strain contains no detectable poly-alpha-L-glutamine in the cell walls and shows marked sensitivity to different chemical and physical stresses such as lysozyme, SDS and sonication. The sensitivity of the mutant to antitubercular drugs, rifampicin and D-cycloserine, is also increased. The glnA-1 strain infects THP-1 cells with reduced efficiency and is also attenuated for growth in macrophages. A Mycobacterium smegmatis strain containing the Mycobacterium bovis glnA-1 gene survives longer in THP-1 cells than the wild-type strain and also produces cell wall-associated poly-alpha-L-glutamine. The mutant is not able to replicate in the organs of BALB/c mice and is cleared within 4-6 weeks of infection. Disruption of the glnA-1 gene adversely affects biofilm formation on polystyrene surfaces
physiological function
-
the C-terminal domain peptide of nod26, a major intrinsic protein that constitutes the major protein component on the symbiosome membrane of N2-fixing soybean nodules, interacts with cytosolic glutamine synthetase GS1beta1. Recombinant soybean GS1beta1 binds the nod26 C-terminal domain with a 1:1 stoichiometry. GS1beta1 also binds to isolated symbiosome membranes, and this binding can be blocked by preincubation with the C-terminal peptide of nod26. In vivo the four cytosolic GS isoforms expressed in soybean nodules interact with full-length nod26
physiological function
hyperthermophilic archaea do not utilize glutamine synthetase predominantly for ammonia assimilation (the major pathway for ammonia assimilation is through glutamate dehydrogenase). The enzyme might play some role in ammonia assimilation under ammonia-starvation conditions
physiological function
glutamine synthetase catalyzes the synthesis of glutamine, providing nitrogen for the production of purines, pyrimidines, amino acids, and other compounds required in many pivotal cellular events. The enzyme is important in the development of the schistosome
physiological function
glutamine synthetase is a key enzyme for root nodule metabolism, and is a molecular target of nitric oxide in root nodules of Medicago truncatula and is regulated by tyrosine nitration. NO-mediated GS posttranslational inactivation is related to metabolite channeling to boost the nodule antioxidant defenses in response to NO
physiological function
-
glutamine synthetase is the only human enzyme responsible for the de novo synthesis of glutamine, catalyzes the reaction of glutamate and ammonia. The enzyme influences sperm motility in mammals
physiological function
-
glutamine synthetase plays a particularly important role in nitrogen metabolism and is the principal source of N for protein and nucleic acid synthesis
physiological function
isozyme OsGS1;1 in the roots is unable to compensate for isozyme OsGS1;2 functions
physiological function
isozyme OsGS1;2 is important in the primary assimilation of ammonium ions taken up by rice roots. Isozyme OsGS1;1 is unable to compensate for isozyme OsGS1;2 functions in roots
physiological function
the enzyme catalyzes the ATP-dependent assimilation of ammonium into glutamate to yield glutamine, which is then used for the biosynthesis of essentially all nitrogenous compounds. Effect of water deprivation varies with variety, degree and duration of stress
physiological function
the enzyme catalyzes the ATP-dependent assimilation of ammonium into glutamate to yield glutamine, which is then used for the biosynthesis of essentially all nitrogenous compounds. Gene OsGS1;1 expression is differently regulated by drought stresss in the two rice Oryza sativa varieties, effect of water deprivation varies with variety, degree and duration of stress
physiological function
the enzyme glutamine synthetase plays an important role in the nitrogen metabolism of fish and in detoxifying ammonia, fish either decrease the production of ammonia, maintain/increase its excretion, or convert ammonia to less toxic products such as glutamine
physiological function
the enzyme is indispensable under excess ammonium conditions. It is required for the resistance of the organism to ammonium accumulation and evasion of the parasitophorous vacuole during host-cell infection. The enzyme contributes to the management of excess ammonium and uses it to form the amino acid glutamine. During its life cycle, the parasite invades mammalian host cells and transiently becomes enclosed in a tight vacuole, where it differentiates into the amastigote, an amino acid consumer stage. Amastigotes must escape from the vacuole into the host-cell cytoplasm to initiate intracellular replication. The inhibition of Trypanosoma cruzi glutamine synthetase aborts parasite evasion from the vacuole. The enzyme contributes to the control of ammonium produced by parasite metabolism, as ammonium increases the internal pH of the parasitophorous vacuole, making the enzymes for the Trypanosoma cruzi evasion process non-functional
physiological function
ammonium is incorporated into carbon skeletons by the sequential action of glutamine synthetase (GS) and glutamate synthase (GOGAT) in cyanobacteria. The activity of Synechocystis sp. PCC 6803 GS type I enzyme is controlled by protein-protein interactions with two intrinsically disordered inactivating factors (IFs): the 65-residue (IF7) and the 149-residue one (IF17), NMR sequence analysis and structure study, overview. The electrostatic-determined binding does not follow a kinetic two-state model, the binding is not diffusion-limited
physiological function
Gln synthetase catalyzes the assimilation of ammonium into Gln and constitutes as such a central component of the N assimilatory pathway in plants. GS2 is the predominant GS isoform in leaves of vegetatively growing plants. In shoots, both GS1 and GS2 contribute to ammonium assimilation into Gln
physiological function
Gln synthetase catalyzes the assimilation of ammonium into Gln and constitutes as such a central component of the N assimilatory pathway in plants. In shoots, both GS1 and GS2 contribute to ammonium assimilation into Gln
physiological function
Gln synthetase catalyzes the assimilation of ammonium into Gln and constitutes as such a central component of the N assimilatory pathway in plants. In shoots, both GS1 and GS2 contribute to ammonium assimilation into Gln. Isozyme Gln-1;2 is essential for ammonium assimilation and amino acid synthesis. Gln-1;2 is the main isozyme contributing to shoot GS1 activity in vegetative growth stages and can be up-regulated to relieve ammonium toxicity
physiological function
glutamine synthetase catalyzes the formation of glutamine from glutamate in the presence of NH4+, ATP, and metal cations. The reaction is the rate-limiting step in the control of N-assimilation and N-recycling during growth and development of plants
physiological function
glutamine synthetase in nodule cytosol plays a major role in the assimilation of the ammonium produced by biological nitrogen fixation
physiological function
glutamine synthetase is an important enzyme that catalyzes the conversion of L-glutamate into L-glutamine and ammonia in an energy dependent reaction with the simultaneous hydrolysis of ATP to ADP. In the cellular system, the enzyme plays an important role in nitrogen metabolism under ammonia-limiting conditions
physiological function
-
glutamine synthetase is one of the key enzymes in nitrogen assimilation, ligating-free ammonium to glutamate to form glutamine and it is therefore crucial for plant growth and productivity
physiological function
glutamine synthetase-mediated autophagy explains the high sensitivity of beta-catenin-active hepatocellular carcinoma cells to sorafenib. beta-Catenin regulates the expression of glutamine synthetase and triggers a series of metabolic changes leading to induction of autophagy in hepatocellular carcinoma cells. Autophagy in beta-catenin-active Hep-3B and Hep-G2 cells is mediated by glutamine synthetase, as silencing of glutamine synthetase significantly reduced autophagic activity
physiological function
specific roles of the individual GS1 isogenes with respect to nitrogen remobilization, early seedling vigour, and final seed productivity. Isozyme Gln1-2 plays an important role in N remobilization for both seedling establishment and seed production in Arabidopsis thaliana
physiological function
specific roles of the individual GS1 isogenes with respect to nitrogen remobilization, early seedling vigour, and final seed productivity. Isozymes Gln1-1 and Gln1-2 play specific roles in seed germination and seedling establishment in Arabidopsis thaliana
physiological function
the enzyme catalyses the ATP-dependent condensation of ammonium and L-glutamate, thus forming L-glutamine, ADP, phosphate and a proton. The enzyme is highly expressed and essential for the growth of the bacteria both in vitro and in vivo. The Mycobacterium tuberculosis enzyme plays an important role in cell wall biosynthesis, specifically via the production of a poly-L-glutamate-glutamine component found exclusively in pathogenic mycobacteria. Extracellular Mycobacterium tuberculosis enzyme may also affect pH modulation in phagosomes and consequently prevent phagosome-lysosome fusion
physiological function
the enzyme catalyzes the ATP-dependent synthesis of L-glutamine from glutamate and ammonia. GlnA1 is also involved in the synthesis of poly-L-glutamate/glutamine for the cell wall of pathogenic mycobacteria
physiological function
-
the rate-limiting step in photorespiration is the reassimilation of ammonia catalyzed by chloroplastic glutamine synthetase isozyme 2 (GS2). In plants, GS2 together with ferredoxin-dependent glutamate synthase (Fd-GOGAT) plays a major role in re-assimilation of ammonium liberated in mitochondria by the glycine decarboxylase, in the pathway known as glutamine synthetase/glutamate synthase (GS/GOGAT) cycle in chloroplasts. The product of this cycle, glutamate, is required for one of the peroxisomal transamination reactions
physiological function
-
glutamine synthetase is an important enzyme that catalyzes the conversion of L-glutamate into L-glutamine and ammonia in an energy dependent reaction with the simultaneous hydrolysis of ATP to ADP. In the cellular system, the enzyme plays an important role in nitrogen metabolism under ammonia-limiting conditions
-
physiological function
-
glutamine synthetase plays a particularly important role in nitrogen metabolism and is the principal source of N for protein and nucleic acid synthesis
-
physiological function
-
hyperthermophilic archaea do not utilize glutamine synthetase predominantly for ammonia assimilation (the major pathway for ammonia assimilation is through glutamate dehydrogenase). The enzyme might play some role in ammonia assimilation under ammonia-starvation conditions
-
physiological function
-
the enzyme is indispensable under excess ammonium conditions. It is required for the resistance of the organism to ammonium accumulation and evasion of the parasitophorous vacuole during host-cell infection. The enzyme contributes to the management of excess ammonium and uses it to form the amino acid glutamine. During its life cycle, the parasite invades mammalian host cells and transiently becomes enclosed in a tight vacuole, where it differentiates into the amastigote, an amino acid consumer stage. Amastigotes must escape from the vacuole into the host-cell cytoplasm to initiate intracellular replication. The inhibition of Trypanosoma cruzi glutamine synthetase aborts parasite evasion from the vacuole. The enzyme contributes to the control of ammonium produced by parasite metabolism, as ammonium increases the internal pH of the parasitophorous vacuole, making the enzymes for the Trypanosoma cruzi evasion process non-functional
-
physiological function
-
the enzyme catalyzes the ATP-dependent synthesis of L-glutamine from glutamate and ammonia. GlnA1 is also involved in the synthesis of poly-L-glutamate/glutamine for the cell wall of pathogenic mycobacteria
-
physiological function
-
the enzyme catalyses the ATP-dependent condensation of ammonium and L-glutamate, thus forming L-glutamine, ADP, phosphate and a proton. The enzyme is highly expressed and essential for the growth of the bacteria both in vitro and in vivo. The Mycobacterium tuberculosis enzyme plays an important role in cell wall biosynthesis, specifically via the production of a poly-L-glutamate-glutamine component found exclusively in pathogenic mycobacteria. Extracellular Mycobacterium tuberculosis enzyme may also affect pH modulation in phagosomes and consequently prevent phagosome-lysosome fusion
-
additional information
the Bacillus subtilis enzyme undergoes dramatic intersubunit conformational alterations during formation of the transition state. Structure-function relationship, overview
additional information
-
the Bacillus subtilis enzyme undergoes dramatic intersubunit conformational alterations during formation of the transition state. Structure-function relationship, overview
additional information
the enzyme sequence contains a classic beta-grasp domain and a catalytic domain of glutamine synthetase
additional information
-
the enzyme sequence contains a classic beta-grasp domain and a catalytic domain of glutamine synthetase
additional information
enzyme structure-activity relationship, overview
additional information
-
enzyme structure-activity relationship, overview
additional information
structure-function relationships of wild-type and mutant enzymes, ligand molecular docking, homology structure modeling using the crystal structure of the enzyme from Bacillus subtilis, PDB ID 4LNF, as a template, overview
additional information
-
structure-function relationships of wild-type and mutant enzymes, ligand molecular docking, homology structure modeling using the crystal structure of the enzyme from Bacillus subtilis, PDB ID 4LNF, as a template, overview
additional information
the C-terminal extension peptide of plastid-located glutamine synthetase from Medicago truncatula is crucial for enzyme activity but needless for protein import into the plastids. The C-terminal extension peptide does not affect the solubility or the stability of the protein but likely the interaction of the enzyme with its substrates. The first 49 amino acids of the N-terminus are predicted to be the transit peptide, the sorting signal for targeting nucleus-encoded proteins to the plastids, which is cleaved during the import
additional information
-
the C-terminal extension peptide of plastid-located glutamine synthetase from Medicago truncatula is crucial for enzyme activity but needless for protein import into the plastids. The C-terminal extension peptide does not affect the solubility or the stability of the protein but likely the interaction of the enzyme with its substrates. The first 49 amino acids of the N-terminus are predicted to be the transit peptide, the sorting signal for targeting nucleus-encoded proteins to the plastids, which is cleaved during the import
additional information
Val161 in GS1beta1 is the key residue responsible for the heat stability
additional information
Val161 in GS1beta1 is the key residue responsible for the heat stability
additional information
-
structure-function relationships of wild-type and mutant enzymes, ligand molecular docking, homology structure modeling using the crystal structure of the enzyme from Bacillus subtilis, PDB ID 4LNF, as a template, overview
-
additional information
-
the Bacillus subtilis enzyme undergoes dramatic intersubunit conformational alterations during formation of the transition state. Structure-function relationship, overview
-
additional information
-
enzyme structure-activity relationship, overview
-
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eicosamer
-
20 * 50000, SDS-PAGE
pentadecamer
structure modelling of a structure consisting of three pentamers, overview
tetramer
-
4 * 43000, minor peak in gel filtration with a mass of 190000 detected for both mutant enzymes
?
x * 40000, about, sequence calculation
?
x * 39300, recombinant His-tagged enzyme, SDS-PAGE
?
-
x * 50000, about, SDS-PAGE
?
x * 70000, fusion-protein with SUMO-tag, SDS-PAGE and calculated
?
-
x * 40000, SDS-PAGE, x * 38759, calculated
?
-
x * 41978, calculation from nucleotide sequence
?
x * 40509, sequence calculation
?
-
x * 51800, sedimentation equilibrium experiments in 6 M urea
?
x * 50100, wild-type enzyme, SDS-PAGE, x * 79600, recombinant GST-tagged wild-type enzyme, SDS-PAGE
?
-
x * 50100, wild-type enzyme, SDS-PAGE, x * 79600, recombinant GST-tagged wild-type enzyme, SDS-PAGE
-
?
x * 40000, about, recombinant His6-tagged isozyme GS1beta1, SDS-PAGE, x * 39399, about, native isozyme, sequence calculation
?
x * 40000, about, recombinant His6-tagged isozyme GS1gamma1, SDS-PAGE, x * 39399, about, native isozyme, sequence calculation
?
-
x * 46691, Unigene0016999, sequence calculation, x * 55408, Unigene0017002, sequence calculation, x * 38300, Unigene0015608, sequence calculation, x * 38750, Unigene0022741, sequence calculation, x * 43909, Unigene0002184, sequence calculation, x * 83726, Unigene0002194, sequence calculation
?
x * 43500, recombinant His-tagged enzyme, SDS-PAGE
?
-
x * 43500, recombinant His-tagged enzyme, SDS-PAGE
-
?
x * 47212, calculated, x * 42000, recombinant protein lacking the target peptide, SDS-PAGE
?
x * 47000, about, full-length wild-type isozyme GS2a, sequence calculation, x * 41700, about, mature and active isozyme GS2a without transit peptide, sequence calculation, x * 40000, about, mutant isozyme GS2a with cleaved N- and C-terminal peptides, sequence calculation
?
x * 45000, calculated from sequence
?
-
x * 45000, calculated from sequence
-
?
x * 46700, about, GlnA3, sequence calculation
?
x * 49600, about, GlnA2, sequence calculation
?
x * 49700, about, GlnA4, sequence calculation
?
x * 53600, about, GlnA1, sequence calculation
?
-
x * 54000, SDS-PAGE
-
?
-
x * 49600, about, GlnA2, sequence calculation
-
?
-
x * 53600, about, GlnA1, sequence calculation
-
?
-
x * 58000, SDS-PAGE
-
?
-
x * 56000, recombinant isozyme GSI
?
-
x * 56000, recombinant isozyme GSI
-
?
-
x * 53348, calculated from sequence
?
-
x * 53348, calculated from sequence
-
?
x * 45000, recombinant enzyme, SDS-PAGE, x * 40700, about, sequence calculation
?
-
x * 42000, isoenzyme GS1, SDS-PAGE
?
-
x * 45000, isoenzyme GS2, SDS-PAGE
?
-
x * 79416, calculation from nucleotide sequence
?
x * 38660, sequence calculation, isozyme GSr2
?
x * 38730, sequence calculation, isozyme GSr1
?
x * 39200, sequence calculation, isozyme GS1a
?
x * 39210, sequence calculation, isozyme GS1a
?
x * 39240, sequence calculation, isozyme GS1c
?
x * 39470, sequence calculation, isozyme GSe2
?
x * 39480, sequence calculation, isozyme GSe1
?
x * 46640, sequence calculation, isozyme GS2b, x * 41710, sequence calculation, mature peptide of isozyme GS2b
?
x * 46690, sequence calculation, isozyme GS2a, x * 41760, sequence calculation, mature peptide of isozyme GS2a
?
x * 46700, sequence calculation, isozyme GS2c, x * 41770, sequence calculation, mature peptide of isozyme GS2c
decamer
10 * 86000, cryo-electron microscopy
decamer
-
10 * 60000, SDS-PAGE
decamer
-
10 * 52000, SDS-PAGE
decamer
-
x-ray crystallography
dimer
-
2 * 83000, recombinant isozyme GSIII-1, SDS-PAGE
dimer
-
2 * 83000, recombinant isozyme GSIII-1, SDS-PAGE
-
dodecamer
-
12 * 60000, SDS-PAGE
dodecamer
-
composed of two hexameric rings
dodecamer
-
type alpha12 dodecamer with oligomer and monomer having molecular weights of 630000 and 52000 Da, respectively
dodecamer
-
composed of two hexameric rings
-
dodecamer
isozyme GSI-alpha
dodecamer
-
isozyme GSI-alpha
-
dodecamer
-
crystallization data
dodecamer
-
12 * 63000, SDS-PAGE
dodecamer
-
12 * 56000, SDS-PAGE
dodecamer
12 * 50500, about, sequence calculation
dodecamer
-
12 * 58000, arranged in two superimpose hexagons, SDS-PAGE
dodecamer
crystal structure analysis, composed of two hexameric rings
dodecamer
Mtb-GlnA1 crystallizes in the space group P212121 with 24 monomers in the asymmetric unit to form a dodecamer. The 24 active sites of the dodecamer are found in long grooves between the subunits
dodecamer
MtGS is a dodecamer formed of two hexameric rings stacked on top of each other. Each active site includes contributions from two adjacent subunits within a ring
dodecamer
-
Mtb-GlnA1 crystallizes in the space group P212121 with 24 monomers in the asymmetric unit to form a dodecamer. The 24 active sites of the dodecamer are found in long grooves between the subunits
-
dodecamer
-
MtGS is a dodecamer formed of two hexameric rings stacked on top of each other. Each active site includes contributions from two adjacent subunits within a ring
-
dodecamer
-
crystal structure analysis, composed of two hexameric rings
-
dodecamer
-
12 * 56000, SDS-PAGE
dodecamer
-
12 * 58000, SDS-PAGE
dodecamer
-
12 * 59000, SDS-PAGE
dodecamer
-
12 * 50100, SDS-PAGE
dodecamer
-
SDS-PAGE of 2-mercaptoethanol-treated enzyme
dodecamer
-
12 * 83000, recombinant isozyme GSIII-1, SDS-PAGE
dodecamer
-
12 * 83000, recombinant isozyme GSIII-1, SDS-PAGE
-
dodecamer
-
12 * 55000, SDS-PAGE
dodecamer
-
12 * 55000, SDS-PAGE
-
dodecamer
-
12 * 55000, the enzyme exhibits different aggregation states with detectable oligomers of 1, 2, 3, 4, 6, 8, 10, and 12 subunits, SDS-PAGE
dodecamer
-
12 * 55000, the enzyme exhibits different aggregation states with detectable oligomers of 1, 2, 3, 4, 6, 8, 10, and 12 subunits, SDS-PAGE
-
dodecamer
12 * 52000, native mass by gel filtration, subunit mass calculated from amino acid sequence
dodecamer
-
12 * 52000, enzyme form GSI, SDS-PAGE
dodecamer
12 * 50088, calculated from sequence
dodecamer
-
12 * 50088, calculated from sequence
-
dodecamer
-
12 * 537000, subunit mass by SDS-PAGE, native structure by negative-stain electron microscopy, consists of two hexameric rings
dodecamer
-
12 * 537000, subunit mass by SDS-PAGE, native structure by negative-stain electron microscopy, consists of two hexameric rings
-
dodecamer
-
12 * 52000, subunit mass by SDS-PAGE, native mass by gel filtration
dodecamer
-
12 * 51000, SDS-PAGE
hexamer
-
6 * 75000, isoform GS2, SDS-PAGE
hexamer
-
6 * 70000, SDS-PAGE
hexamer
-
6 * 70000, SDS-PAGE
-
hexamer
-
6 * 80000, enzyme form GSIII, SDS-PAGE
homooctamer
-
8 * 44000, SDS-PAGE
homooctamer
-
8 * 44000, SDS-PAGE
monomer
the enzyme is present in solution as monomer and as oligomer
monomer
-
the enzyme is present in solution as monomer and as oligomer
-
octamer
-
8 * 43000, isoform GSII, SDS-PAGE
octamer
-
8 * 47000, isoform GSI, SDS-PAGE
octamer
-
8 * 51700, gel filtration
octamer
-
8 * 44000, SDS-PAGE, composed of three different types of subunits with isoelectric points ranging from 7.0-7.2
octamer
-
8 * 37400, subunit mass by SDS-PAGE, native mass by native PAGE
octamer
-
8 * 43000, subunits by SDS-PAGE, native mass by gel filtration
octamer
8 * 42400, SDS-PAGE
octamer
8 * 43000, gel filtration
octamer
-
8 * 48000, isoenzyme GScs, SDS-PAGE
octamer
-
8 * 64000, isoenzyme GScl, SDS-PAGE
octamer
-
8 * 48000, isoform GS2, SDS-PAGE
octamer
-
8 * 38000, isoform GS1, SDS-PAGE
octamer
-
x * 46500 + x * 49000, SDS-PAGE
octamer
-
alpha, beta, 4 * 58000 + 4 * 65000, native mass by gel filtration, subunit mass by SDS-PAGE
octamer
-
8 * 44000, enzyme form GS2, SDS-PAGE
oligomer
the enzyme is present in solution as monomer and as oligomer
oligomer
-
the enzyme is present in solution as monomer and as oligomer
-
trimer
-
3 * 83000, recombinant isozyme GSIII-2, SDS-PAGE
trimer
-
3 * 83000, recombinant isozyme GSIII-2, SDS-PAGE
-
additional information
structure analysis, and comparison of mammalian, plant, and bacterial structures, overview
additional information
-
structure analysis, and comparison of mammalian, plant, and bacterial structures, overview
additional information
-
structure analysis, and comparison of mammalian, plant, and bacterial structures, overview
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glnADELTA
no detectable glutamine synthetase activity
A174S
isoenzyme GLN1,3, 3.6fold increase in ratio of turnover-number to KM-value for NH4+
K49Q
isoenzyme GLN1,3, 3fold increase in ratio of turnover-number to KM-value for NH4+
K49Q/A174S
isoenzyme GLN1,3, 2.8fold increase in ratio of turnover-number to KM-value for NH4+
Q49K
isoenzyme GLN1,4, 2.2fold decrease in ratio of turnover-number to KM-value for NH4+
Q49K/S174A
isoenzyme GLN1,4, 6.8fold increase in ratio of turnover-number to KM-value for NH4+
S174A
isoenzyme GLN1,4, 1.3fold increase in ratio of turnover-number to KM-value for NH4+
A305G
-
mutation in the E304 flap, a flexible 7-residue loop over the entrance to the active site. 16% of wild-type activity with L-glutamate, 2% of wild-type activity with L-glutamine
E304A/A305G
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
E304D
-
mutation in the E304 flap, a flexible 7-residue loop over the entrance to the active site. 37% of wild-type activity with L-glutamate, 8% of wild-type activity with L-glutamine
E304H
-
mutation in the E304 flap, a flexible 7-residue loop over the entrance to the active site. 43% of wild-type activity with L-glutamate, 5% of wild-type activity with L-glutamine
E424K
-
the mutant enzyme is defective in its ability to interact with GlnR
G302A
-
mutation in the E304 flap, a flexible 7-residue loop over the entrance to the active site. 80% of wild-type activity with L-glutamate, 58% of wild-type activity with L-glutamine
P306A
-
mutation in the E304 flap, a flexible 7-residue loop over the entrance to the active site. 160% of wild-type activity with L-glutamate, 130% of wild-type activity with L-glutamine
R62A
site-directed mutagenesis, the mutation abrogates Gln feedback inhibition but does not affect catalysis
V300A
-
mutation in the E304 flap, a flexible 7-residue loop over the entrance to the active site. 76% of wild-type activity with L-glutamate, 18% of wild-type activity with L-glutamine
Y303A
-
mutation in the E304 flap, a flexible 7-residue loop over the entrance to the active site. 36% of wild-type activity with L-glutamate, 8% of wild-type activity with L-glutamine
Y303H
-
mutation in the E304 flap, a flexible 7-residue loop over the entrance to the active site. 150% of wild-type activity with L-glutamate, 100% of wild-type activity with L-glutamine
Y303L
-
mutation in the E304 flap, a flexible 7-residue loop over the entrance to the active site. 87% of wild-type activity with L-glutamate, 46% of wild-type activity with L-glutamine
E304A/A305G
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
-
R62A
-
site-directed mutagenesis, the mutation abrogates Gln feedback inhibition but does not affect catalysis
-
D50E
-
mutant D50E shows activity with Mn2+ but very low activity with Mg2+, and altered kcat/Km values for all three substrates. Mutant E327A has a decreased kcat/Km value for NH4+ compared to that of the wild-type enzyme. Asp-50 is likely involved in binding NH4+ and may also play a role in catalyzing deprotonation of NH4+ to form NH3. Glu-327 participates in lowering the free energy of the transition state involved in formation of the positively charged tetrahedral adduct resulting from the condensation of gamma-glutamyl phosphate and NH3
E165C
-
mutant yields inter-subunit disulfide bonds connecting central loops. Inter-subunit disulfide bonds between the central loops causes no detectable changes in the KM-values for glutamate or ATP, nor the KD for either ATP or the transition state analog L-methionine sulfoximine. Covalent and quantitative adduction of the E165C mutant with iodo-acetamido-pyrene yields nearly fully active enzyme
H12D
-
each of the mutant proteins H4A, H4C, M8L, H12L, H12D retains an intact dodecameric ring structure and no significant changes in catalytic and regulatory behavior are caused by the amino acid substitutions on the dodecamer surface. The substitution Ala4His completely abolishes the (NH4)2SO4-induced aggregation. However the H4C mutant protein precipitates nearly completely under the same salting out conditions
H12L
-
each of the mutant proteins H4A, H4C, M8L, H12L, H12D retains an intact dodecameric ring structure and no significant changes in catalytic and regulatory behavior are caused by the amino acid substitutions on the dodecamer surface. The substitution Ala4His completely abolishes the (NH4)2SO4-induced aggregation. However the H4C mutant protein precipitates nearly completely under the same salting out conditions
H4A
-
each of the mutant proteins H4A, H4C, M8L, H12L, H12D retains an intact dodecameric ring structure and no significant changes in catalytic and regulatory behavior are caused by the amino acid substitutions on the dodecamer surface. The substitution Ala4His completely abolishes the (NH4)2SO4-induced aggregation. However the H4C mutant protein precipitates nearly completely under the same salting out conditions
H4C
-
each of the mutant proteins H4A, H4C, M8L, H12L, H12D retains an intact dodecameric ring structure and no significant changes in catalytic and regulatory behavior are caused by the amino acid substitutions on the dodecamer surface. The substitution Ala4His completely abolishes the (NH4)2SO4-induced aggregation. However the H4C mutant protein precipitates nearly completely under the same salting out conditions
M8L
-
each of the mutant proteins H4A, H4C, M8L, H12L, H12D retains an intact dodecameric ring structure and no significant changes in catalytic and regulatory behavior are caused by the amino acid substitutions on the dodecamer surface. The substitution Ala4His completely abolishes the (NH4)2SO4-induced aggregation. However the H4C mutant protein precipitates nearly completely under the same salting out conditions
Y397A
-
mutant enzyme behaves as if it is adenylated
Y397F
-
the specific activity is almost double that of the wild-type enzyme, mutant enzyme behaves as if it is unadenylated
Y397S
-
mutant enzyme behaves as if it is adenylated
E60A
site-directed mutagenesis, the E60A mutant has about 2.2fold increased activity compared to wild-type
E60A/R64G
site-directed mutagenesis, no significant change is observed in the activity of E60A/R64G mutant
F239Y
site-directed mutagenesis, the mutant has slightly reduced activity compared to wild-type
P135S
site-directed mutagenesis, the mutant has slightly reduced activity compared to wild-type
R64G
site-directed mutagenesis, the binding pocket undergoes dramatic changes when Arg site of 64 is substituted by Gly, thus promoting the rapid capture of substrates and leading to increase in activity and PPT-resistance of mutant R64G. Kinetic analysis shows that the kcat of R64G mutant is increased by 8.10, 7.25 and 7.63fold for ADP, glutamine and hydroxylamine, respectively, the mutant has about 1.9fold increased activity compared to wild-type
V241D
site-directed mutagenesis, the mutant has slightly increased activity compared to wild-type
Y305F
site-directed mutagenesis, the mutant has reduced activity compared to wild-type
Y375P
site-directed mutagenesis, the mutant has slightly increased activity compared to wild-type
E60A
-
site-directed mutagenesis, the E60A mutant has about 2.2fold increased activity compared to wild-type
-
E60A/R64G
-
site-directed mutagenesis, no significant change is observed in the activity of E60A/R64G mutant
-
P135S
-
site-directed mutagenesis, the mutant has slightly reduced activity compared to wild-type
-
R64G
-
site-directed mutagenesis, the binding pocket undergoes dramatic changes when Arg site of 64 is substituted by Gly, thus promoting the rapid capture of substrates and leading to increase in activity and PPT-resistance of mutant R64G. Kinetic analysis shows that the kcat of R64G mutant is increased by 8.10, 7.25 and 7.63fold for ADP, glutamine and hydroxylamine, respectively, the mutant has about 1.9fold increased activity compared to wild-type
-
Y305F
-
site-directed mutagenesis, the mutant has reduced activity compared to wild-type
-
Y167F
site-directed mutagenesis of isozyme MtGS1a reduces the inhibition by tetranitromethane
D56A
-
complete loss of activity in reverse reaction, 83% of wild-type activity in forward reaction, salting out at much higher ammonium sulfate concentrations than wild type enzyme
D56E
-
complete loss of activity in reverse reaction, 65% of wild-type activity in forward reaction, salting out properties only slightly affected
E297A
-
Km for ammonium strongly increased, minor effects on activity in forward reaction, reverse reaction activity strongly decreased, strong effect on binding behavior to a 2',5'-ADP-sepharose
E152A
mutant enzyme shows decreased enzymatic activity
E192A
mutant enzyme shows decreased enzymatic activity
E194A
mutant enzyme shows decreased enzymatic activity
E308A
mutation results in an increase in activity in the forward assay compared to wild-type enzyme
E380A
mutant enzyme shows decreased enzymatic activity
E77A
no difference to wild-type enzyme in activity
K318A
mutant enzyme shows decreased enzymatic activity
E152A
-
mutant enzyme shows decreased enzymatic activity
-
E192A
-
mutant enzyme shows decreased enzymatic activity
-
E194A
-
mutant enzyme shows decreased enzymatic activity
-
E308A
-
mutation results in an increase in activity in the forward assay compared to wild-type enzyme
-
E77A
-
no difference to wild-type enzyme in activity
-
D51A
7% of activity in forward reaction, 4% of activity in reverse reaction no effect on protein structure
D51E
5% of activity in forward reaction, 87% of activity in reverse reaction no effect on protein structure
D51N
1.7% of activity in forward reaction, 2.4% of activity in reverse reaction no effect on protein structure
D51R
complete loss of activity, no effect on protein structure
D51S
24% of activity in forward reaction, 15% of activity in reverse reaction, no effect on protein structure
S186F
-
kinetic properties are similar to the wild-type protein, mutant S186F enzyme is resistant to feedback inhibition by glutamine and AMP. S186F protein has a lower affinity for glutamine and AMP than the wild-type enzyme. S186F glutamine synthetase is defective in its ability to block DNA binding by TnrA in vitro
S186F
-
the mutant enzyme is defective in its ability to interact with GlnR
Y404F
mutant lacks adenylylation
Y404F
-
mutant lacks adenylylation
-
gln1-3gln1-4 mutant
74% decrease in GS1 activity compared to the wild type enzyme
gln1-3gln1-4 mutant
increased GS2 activity compared to the wild type enzyme
gln1-3mutant
45% decrease in GS1 activity compared to the wild type enzyme
gln1-3mutant
increased GS2 activity compared to the wild type enzyme
gln1-4 mutant
16% decrease in GS1 activity compared to the wild type enzyme
gln1-4 mutant
increased GS2 activity compared to the wild type enzyme
additional information
generation of a double knockout mutant gln1-1:gln1-2
additional information
generation of a double knockout mutant gln1-1:gln1-2
additional information
generation of a single knockout mutant gln1-2 and a double knockout mutant gln1-1:gln1-2
additional information
generation of a single knockout mutant gln1-2 and a double knockout mutant gln1-1:gln1-2
additional information
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the phenotype of the single mutant gln1;1 is similar to the wild-type, while the double mutant gln1;1:gln1;2 shows a growth that is significantly impaired irrespective of N regime
additional information
the phenotype of the single mutant gln1;1 is similar to the wild-type, while the double mutant gln1;1:gln1;2 shows a growth that is significantly impaired irrespective of N regime
additional information
the phenotype of the single mutant gln1;1 is similar to the wild-type, while the double mutant gln1;1:gln1;2 shows a growth that is significantly impaired irrespective of N regime
additional information
-
the phenotype of the single mutant gln1;2 and double mutant gln1;1:gln1;2 shows a growth that is significantly impaired irrespective of N regime. The GS1 enzyme activity is significantly reduced in both gln1;2 and gln1;1:gln1;2. Along with this, the ammonium content increases while that of Gln decreases
additional information
the phenotype of the single mutant gln1;2 and double mutant gln1;1:gln1;2 shows a growth that is significantly impaired irrespective of N regime. The GS1 enzyme activity is significantly reduced in both gln1;2 and gln1;1:gln1;2. Along with this, the ammonium content increases while that of Gln decreases
additional information
the phenotype of the single mutant gln1;2 and double mutant gln1;1:gln1;2 shows a growth that is significantly impaired irrespective of N regime. The GS1 enzyme activity is significantly reduced in both gln1;2 and gln1;1:gln1;2. Along with this, the ammonium content increases while that of Gln decreases
additional information
isozyme GmGS1beta1 can complement the Escherichia coli Gln-auxotrophic strain JW3841-1 effectively at 37°C
additional information
isozyme GmGS1beta1 can complement the Escherichia coli Gln-auxotrophic strain JW3841-1 effectively at 37°C
additional information
isozyme GmGS1gamma1 is unable to complement the Escherichia coli Gln-auxotrophic strain JW3841-1 effectively at 37°C. The lack of active GmGS1gamma1 production for the successful complementation at 37°C can be attributed to misfolding or conformational instability caused by increased temperature
additional information
isozyme GmGS1gamma1 is unable to complement the Escherichia coli Gln-auxotrophic strain JW3841-1 effectively at 37°C. The lack of active GmGS1gamma1 production for the successful complementation at 37°C can be attributed to misfolding or conformational instability caused by increased temperature
additional information
identification of single nucleotide polymorphisms of the genomic GhGS sequences in 7235 and TM-1
additional information
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identification of single nucleotide polymorphisms of the genomic GhGS sequences in 7235 and TM-1
additional information
-
enzyme-deficient cells show altered cell proliferation rates compared to the wild-type or enzyme overexpressing cells, overview
additional information
generation of glutamine synthetase-silenced Hep-3B cells by transduction with two independent shRNAs, and glutamine synthetase-overexpressing SK-Hep-1 cells
additional information
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determination and photosynthetic responses of GS2 mutant of barley with reduced activity of chloroplastic glutamine synthetase, overview. The mutation of the enzyme not directly associated with conversion of light energy leads to significant modifications of structure and function of photosystems
additional information
functional expression in a yeast mutant deficient in glutamine synthetase activity restores growth of the yeast mutant on media containing ammonium as the sole N source
additional information
functional expression in a yeast mutant deficient in glutamine synthetase activity restores growth of the yeast mutant on media containing ammonium as the sole N source
additional information
-
functional expression in a yeast mutant deficient in glutamine synthetase activity restores growth of the yeast mutant on media containing ammonium as the sole N source
additional information
generation of a construct, MtGS2DELTACT, encoding MtGS2a mature protein (without the N-terminal plastid targeting signal) truncated at the C-terminal (lacking the last 16 amino acid residues) and with a hexahistidine tag (His-tag) fused to the N-terminal in the pET28a expression vector. The solubility and the thermal stability of MtGS2a proteins with and without the C-terminal extension peptide are similar. The specific activity of the recombinant protein without the C-terminal extension peptide, either transferase or syntethase activity, is lower compared with that of the protein with the C-terminal extension peptide
additional information
-
generation of a construct, MtGS2DELTACT, encoding MtGS2a mature protein (without the N-terminal plastid targeting signal) truncated at the C-terminal (lacking the last 16 amino acid residues) and with a hexahistidine tag (His-tag) fused to the N-terminal in the pET28a expression vector. The solubility and the thermal stability of MtGS2a proteins with and without the C-terminal extension peptide are similar. The specific activity of the recombinant protein without the C-terminal extension peptide, either transferase or syntethase activity, is lower compared with that of the protein with the C-terminal extension peptide
additional information
-
glnA1 mutants are attenuated for intracellular growth in human THP-1 macrophages and are unable to infect guinea pigs
additional information
-
glnA1 mutants are attenuated for intracellular growth in human THP-1 macrophages and are unable to infect guinea pigs
-
additional information
a glnA2 mutant provides protection against infection with virulent Mycobacterium bovis
additional information
a glnA2 mutant provides protection against infection with virulent Mycobacterium bovis
additional information
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a glnA2 mutant provides protection against infection with virulent Mycobacterium bovis
additional information
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a glnA2 mutant provides protection against infection with virulent Mycobacterium bovis
-
additional information
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recombinant transient expression of transcription factor PpDof5 from Pinus pinaster, using infiltration with Agrobacterium tumefaciens cells, the recombinant protein regulates the expression of isozymes GS1a and GS1b promoters in tobacco leaves, overview
additional information
generation of knockout mutants by the insertion of an endogenous retrotransposon Tos17 into exon 2 of OsGS1;2
additional information
generation of knockout mutants by the insertion of an endogenous retrotransposon Tos17 into exon 2 of OsGS1;2
additional information
generation of knockout mutants by the insertion of an endogenous retrotransposon Tos17 into exon 2 of OsGS1;2
additional information
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two genes encode glutamine synthetase, glnN and glnA. GlnN supports Synechocystis growth in a strain whose glnA gene is inactivated by insertional mutagenesis
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