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ATP + acetyl-Cys + Gly
ADP + phosphate + acetyl-Cys-Gly
-
-
-
-
?
ATP + beta-aminoglutaryl-L-2-aminobutyrate + Gly
ADP + phosphate + beta-aminoglutaryl-L-2-aminobutyryl-Gly
ATP + DL-gamma-(beta-methyl)Glu-L-2-aminobutyrate + Gly
ADP + phosphate + DL-gamma-(beta-methyl)Glu-L-2-aminobutyryl-Gly
-
44% of the activity relative to L-gamma-Glu-L-2-aminobutyrate
-
-
?
ATP + DL-gamma-(gamma-methyl)Glu-L-2-aminobutyrate + Gly
ADP + phosphate + DL-gamma-(gamma-methyl)Glu-L-2-aminobutyryl-Gly
-
16% of the activity relative to L-gamma-Glu-L-2-aminobutyrate
-
-
?
ATP + gamma-(alpha-aminomethyl)Glu-2-aminobutyrate + Gly
ADP + phosphate + gamma-Glu-L-2-aminopentanoyl-Gly
-
-
-
-
?
ATP + gamma-Glu-2-aminobutyrate + hydroxylamine
ADP + phosphate + gamma-(alpha-aminomethyl)Glu-2-aminobutyryl-Gly
ATP + gamma-Glu-aminobutyrate + Gly
ADP + phosphate + ophthalmic acid
ATP + gamma-Glu-L-Cys + Ala
ADP + phosphate + gamma-Glu-Cys-Ala
ATP + gamma-Glu-L-Cys + aminomethanesulfonic acid
ADP + phosphate + gamma-Glu-L-Cys-aminomethanesulfonic acid
Pigeon
-
-
-
-
?
ATP + gamma-Glu-L-Cys + aminooxyacetate
ADP + phosphate + gamma-Glu-Cys-aminoxyacetate
-
53% of the activity relative to Gly
-
-
?
ATP + gamma-Glu-L-Cys + Gly
?
ATP + gamma-Glu-L-Cys + Gly
ADP + phosphate + gamma-glutathione
ATP + gamma-Glu-L-Cys + Gly
ADP + phosphate + glutathione
ATP + gamma-Glu-L-Cys + N-hydroxyglycine
ADP + phosphate + gamma-Glu-Cys-N-hydroxyglycine
-
33% of the activity relative to Gly
-
-
?
ATP + gamma-Glu-L-Cys + Ser
ADP + phosphate + gamma-Glu-Cys-Ser
-
-
-
-
?
ATP + gamma-Glu-S-methylcysteine + Gly
ADP + phosphate + gamma-Glu-S-methylcysteinyl-Gly
ATP + gamma-glutamyl-alpha-aminobutyrate
?
-
-
-
?
ATP + gamma-L-Glu-aminobutanoate + Gly
ADP + phosphate + ophthalmic acid
-
-
-
-
?
ATP + gamma-L-Glu-L-alpha-aminobutyrate + Gly
ADP + phosphate + glutathione
-
-
-
r
ATP + gamma-L-Glu-L-Cys + 3-amino-1-propanol
ADP + phosphate + L-gamma-glutamyl-N-(3-hydroxypropyl)-L-cysteinamide
ATP + gamma-L-Glu-L-Cys + alpha-aminobutyric acid
ADP + phosphate + gamma-Glu-L-Cys-alpha-aminobutyric acid
-
-
-
?
ATP + gamma-L-Glu-L-Cys + beta-Ala
ADP + phosphate + gamma-Glu-L-Cys-beta-Ala
ATP + gamma-L-Glu-L-Cys + beta-Ala
ADP + phosphate + gamma-L-Glu-L-Cys-beta-Ala
no activity with D-Ala
-
-
?
ATP + gamma-L-Glu-L-Cys + beta-aminoisobutyric acid
ADP + phosphate + gamma-Glu-L-Cys-beta-aminoisobutyric acid
ATP + gamma-L-Glu-L-Cys + beta-aminoisobutyric acid
ADP + phosphate + gamma-L-Glu-L-Cys-beta-aminoisobutyric acid
-
-
-
?
ATP + gamma-L-Glu-L-Cys + D-Ala
ADP + phosphate + gamma-Glu-L-Cys-D-Ala
ATP + gamma-L-Glu-L-Cys + D-Ser
ADP + phosphate + gamma-Glu-L-Cys-D-Ser
ATP + gamma-L-Glu-L-Cys + ethanolamine
ADP + phosphate + gamma-Glu-L-Cys-ethanolamine
ATP + gamma-L-Glu-L-Cys + gamma-aminobutyric acid
ADP + phosphate + gamma-Glu-L-Cys-gamma-aminobutyric acid
ATP + gamma-L-Glu-L-Cys + gamma-aminobutyric acid
ADP + phosphate + gamma-L-Glu-L-Cys-gamma-aminobutyric acid
-
-
-
?
ATP + gamma-L-Glu-L-Cys + Gly
ADP + phosphate + glutathione
ATP + gamma-L-Glu-L-Cys + L-2,3-diaminopropionic acid
ADP + phosphate + gamma-Glu-L-Cys-L-2,3-diaminopropionic acid
ATP + gamma-L-Glu-L-Cys + L-2,3-diaminopropionic acid
ADP + phosphate + gamma-L-Glu-L-Cys-L-2,3-diaminopropionic acid
-
-
-
?
ATP + gamma-L-Glu-L-Cys + L-Ala
ADP + phosphate + gamma-Glu-L-Cys-L-Ala
ATP + gamma-L-Glu-L-Cys + L-Ala
ADP + phosphate + gamma-L-Glu-L-Cys-L-Ala
no activity with D-Ala
-
-
?
ATP + gamma-L-Glu-L-Cys + L-Orn
ADP + phosphate + gamma-Glu-L-Cys-L-Orn
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
ATP + Glu-L-2-aminobutyrate + Gly
ADP + phosphate + gamma-Glu-L-Cys-Gly
-
16% of the activity relative to L-gamma-Glu-L-2-aminobutyrate
-
-
?
ATP + L-gamma-(alpha-methyl)Glu-L-2-aminobutyrate + Gly
ADP + phosphate + L-gamma-(alpha-methyl)Glu-L-2-aminobutyryl-Gly
-
-
-
-
?
ATP + L-gamma-(N-methyl)Glu-L-2-aminobutyrate + Gly
ADP + phosphate + L-gamma-(N-methyl)Glu-L-2-aminobutyryl-Gly
-
52% of the activity relative to L-gamma-Glu-L-2-aminobutyrate
-
-
?
ATP + L-gamma-Glu-Gly + Gly
ADP + phosphate + L-gamma-Glu-Gly-Gly
-
8% of the activity relative to L-gamma-Glu-L-2-aminobutyrate
-
-
?
ATP + L-gamma-Glu-L-2-aminopentanoic acid + Gly
ADP + phosphate + gamma-Glu-S-methylcysteinyl-Gly
-
9% of the activity relative to L-gamma-Glu-L-2-aminobutyrate
-
-
?
ATP + L-gamma-Glu-L-Ala + Gly
ADP + phosphate + L-gamma-Glu-L-Ala-Gly
-
55% of the activity relative to L-gamma-Glu-L-2-aminobutyrate
-
-
?
ATP + L-gamma-Glu-L-Cys + Gly
ADP + phosphate + L-gamma-Glu-L-Cys-Gly
-
102% of the activity relative to L-gamma-Glu-L-2-aminobutyrate
-
-
?
ATP + L-gamma-Glu-L-Ser + Gly
ADP + phosphate + L-gamma-Glu-L-Ser-Gly
-
77% of the activity relative to L-gamma-Glu-L-2-aminobutyrate
-
-
?
ATP + L-gamma-glutamyl-L-alpha-aminobutyrate + glycine
ADP + L-gamma-glutamyl-L-alpha-aminobutyryl-glycine
gamma-GluABA, an analogue of gamma-L-glutamyl-L-cysteine (gamma-GC) with the same activity and kinetic properties as gamma-GC
-
-
?
ATP + N-acetyl-L-2-aminobutyrate + Gly
ADP + phosphate + N-acetyl-L-2-aminobutyrate-Gly
-
8% of the activity relative to L-gamma-glutamyl-L-2-aminobutyrate
-
-
?
ATP + N-acetyl-L-Cys + Gly
ADP + phosphate + N-acetyl-L-Cys-Gly
-
20% of the activity relative to L-gamma-Glu-L-2-aminobutyrate
-
-
?
CTP + gamma-Glu-L-Cys + Gly
CDP + phosphate + glutathione
-
4% of the activity relative to ATP
-
-
?
dATP + gamma-Glu-L-Cys + Gly
dADP + phosphate + glutathione
gamma-L-glutamyl-L-cysteine + glycine + ATP
ADP + phosphate + glutathione
-
-
-
?
glycine + ATP + gamma-L-glutamyl-L-cysteine
ADP + phosphate + glutathione
-
assay at pH 8.2
-
-
?
GTP + gamma-Glu-L-Cys + Gly
GDP + phosphate + glutathione
-
3% of the activity relative to ATP
-
-
?
ITP + gamma-Glu-L-Cys + Gly
IDP + phosphate + glutathione
-
6% of the activity relative to ATP
-
-
?
UTP + gamma-Glu-L-Cys + Gly
UDP + phosphate + glutathione
additional information
?
-
ATP + beta-aminoglutaryl-L-2-aminobutyrate + Gly
ADP + phosphate + beta-aminoglutaryl-L-2-aminobutyryl-Gly
-
-
-
-
?
ATP + beta-aminoglutaryl-L-2-aminobutyrate + Gly
ADP + phosphate + beta-aminoglutaryl-L-2-aminobutyryl-Gly
-
15% of the activity relative to L-gamma-Glu-L-2-aminobutyrate
-
-
?
ATP + gamma-Glu-2-aminobutyrate + hydroxylamine
ADP + phosphate + gamma-(alpha-aminomethyl)Glu-2-aminobutyryl-Gly
-
-
-
-
?
ATP + gamma-Glu-2-aminobutyrate + hydroxylamine
ADP + phosphate + gamma-(alpha-aminomethyl)Glu-2-aminobutyryl-Gly
-
-
-
-
?
ATP + gamma-Glu-aminobutyrate + Gly
ADP + phosphate + ophthalmic acid
-
-
-
?
ATP + gamma-Glu-aminobutyrate + Gly
ADP + phosphate + ophthalmic acid
-
-
-
-
?
ATP + gamma-Glu-aminobutyrate + Gly
ADP + phosphate + ophthalmic acid
-
L-gamma-Glu-L-2-aminobutyrate
-
-
?
ATP + gamma-Glu-aminobutyrate + Gly
ADP + phosphate + ophthalmic acid
-
D-gamma-Glu-L-2-aminobutyrate
-
-
?
ATP + gamma-Glu-aminobutyrate + Gly
ADP + phosphate + ophthalmic acid
-
-
-
-
?
ATP + gamma-Glu-aminobutyrate + Gly
ADP + phosphate + ophthalmic acid
-
-
-
?
ATP + gamma-Glu-L-Cys + Ala
ADP + phosphate + gamma-Glu-Cys-Ala
-
beta-alanine
-
-
?
ATP + gamma-Glu-L-Cys + Ala
ADP + phosphate + gamma-Glu-Cys-Ala
-
-
-
-
?
ATP + gamma-Glu-L-Cys + Gly
?
-
glutathione biosynthesis
-
-
?
ATP + gamma-Glu-L-Cys + Gly
?
-
-
-
-
?
ATP + gamma-Glu-L-Cys + Gly
?
-
-
-
-
?
ATP + gamma-Glu-L-Cys + Gly
?
-
-
-
-
?
ATP + gamma-Glu-L-Cys + Gly
ADP + phosphate + gamma-glutathione
-
-
ir
ATP + gamma-Glu-L-Cys + Gly
ADP + phosphate + gamma-glutathione
-
-
ir
ATP + gamma-Glu-L-Cys + Gly
ADP + phosphate + gamma-glutathione
-
-
-
ir
ATP + gamma-Glu-L-Cys + Gly
ADP + phosphate + glutathione
-
-
-
-
?
ATP + gamma-Glu-L-Cys + Gly
ADP + phosphate + glutathione
-
-
-
?
ATP + gamma-Glu-L-Cys + Gly
ADP + phosphate + glutathione
random ter-reactant mechanism, ADP is the last product released
-
-
?
ATP + gamma-Glu-L-Cys + Gly
ADP + phosphate + glutathione
-
-
-
-
?
ATP + gamma-Glu-L-Cys + Gly
ADP + phosphate + glutathione
-
-
-
ir
ATP + gamma-Glu-L-Cys + Gly
ADP + phosphate + glutathione
Brettanomyces abstinens
-
-
-
-
?
ATP + gamma-Glu-L-Cys + Gly
ADP + phosphate + glutathione
-
-
-
-
?
ATP + gamma-Glu-L-Cys + Gly
ADP + phosphate + glutathione
-
-
-
-
?
ATP + gamma-Glu-L-Cys + Gly
ADP + phosphate + glutathione
-
-
-
-
?
ATP + gamma-Glu-L-Cys + Gly
ADP + phosphate + glutathione
-
-
1187, 1189, 1192, 1197, 1205, 1208, 1209, 1210, 1212, 1215, 1216, 1217, 1218, 1219, 1220 -
-
?
ATP + gamma-Glu-L-Cys + Gly
ADP + phosphate + glutathione
-
-
-
ir
ATP + gamma-Glu-L-Cys + Gly
ADP + phosphate + glutathione
-
-
-
?
ATP + gamma-Glu-L-Cys + Gly
ADP + phosphate + glutathione
-
-
i.e. gamma-Glu-Cys-Gly
?
ATP + gamma-Glu-L-Cys + Gly
ADP + phosphate + glutathione
-
-
i.e. gamma-Glu-Cys-Gly
?
ATP + gamma-Glu-L-Cys + Gly
ADP + phosphate + glutathione
-
-
-
-
?
ATP + gamma-Glu-L-Cys + Gly
ADP + phosphate + glutathione
-
-
i.e. gamma-Glu-Cys-Gly
?
ATP + gamma-Glu-L-Cys + Gly
ADP + phosphate + glutathione
-
-
-
-
?
ATP + gamma-Glu-L-Cys + Gly
ADP + phosphate + glutathione
-
-
-
-
?
ATP + gamma-Glu-L-Cys + Gly
ADP + phosphate + glutathione
-
-
-
?
ATP + gamma-Glu-L-Cys + Gly
ADP + phosphate + glutathione
patients with hereditary glutathione synthetase deficiency suffer from haemolytic anaemia, 5-oxoprolinuria, metabolic acidosis, recurrent bacterial infections and various degrees of central nervous system dysfunction
-
-
?
ATP + gamma-Glu-L-Cys + Gly
ADP + phosphate + glutathione
two NFE2 sites in the human GSS promoter play important roles in the basal expression of glutathione synthetase. The glutathione synthetase gene expression is also regulated by Nrf2
-
-
?
ATP + gamma-Glu-L-Cys + Gly
ADP + phosphate + glutathione
-
-
-
-
?
ATP + gamma-Glu-L-Cys + Gly
ADP + phosphate + glutathione
-
-
-
-
?
ATP + gamma-Glu-L-Cys + Gly
ADP + phosphate + glutathione
-
-
-
-
?
ATP + gamma-Glu-L-Cys + Gly
ADP + phosphate + glutathione
-
-
-
-
?
ATP + gamma-Glu-L-Cys + Gly
ADP + phosphate + glutathione
-
-
-
-
?
ATP + gamma-Glu-L-Cys + Gly
ADP + phosphate + glutathione
-
-
-
-
?
ATP + gamma-Glu-L-Cys + Gly
ADP + phosphate + glutathione
Pigeon
-
-
-
-
?
ATP + gamma-Glu-L-Cys + Gly
ADP + phosphate + glutathione
-
-
-
-
?
ATP + gamma-Glu-L-Cys + Gly
ADP + phosphate + glutathione
-
-
-
-
?
ATP + gamma-Glu-L-Cys + Gly
ADP + phosphate + glutathione
-
-
-
-
?
ATP + gamma-Glu-L-Cys + Gly
ADP + phosphate + glutathione
-
-
i.e. gamma-Glu-Cys-Gly
?
ATP + gamma-Glu-L-Cys + Gly
ADP + phosphate + glutathione
Saccharomyces pombe
-
-
-
-
?
ATP + gamma-Glu-L-Cys + Gly
ADP + phosphate + glutathione
-
-
-
-
?
ATP + gamma-Glu-L-Cys + Gly
ADP + phosphate + glutathione
-
-
-
-
?
ATP + gamma-Glu-L-Cys + Gly
ADP + phosphate + glutathione
-
-
-
-
?
ATP + gamma-Glu-L-Cys + Gly
ADP + phosphate + glutathione
-
-
-
?
ATP + gamma-Glu-L-Cys + Gly
ADP + phosphate + glutathione
-
-
-
?
ATP + gamma-Glu-L-Cys + Gly
ADP + phosphate + glutathione
-
-
-
-
?
ATP + gamma-Glu-L-Cys + Gly
ADP + phosphate + glutathione
-
-
-
?
ATP + gamma-Glu-L-Cys + Gly
ADP + phosphate + glutathione
-
-
i.e. gamma-Glu-Cys-Gly
?
ATP + gamma-Glu-S-methylcysteine + Gly
ADP + phosphate + gamma-Glu-S-methylcysteinyl-Gly
-
-
-
-
?
ATP + gamma-Glu-S-methylcysteine + Gly
ADP + phosphate + gamma-Glu-S-methylcysteinyl-Gly
-
24% of the activity relative to L-gamma-Glu-L-2-aminobutyrate
-
-
?
ATP + gamma-L-Glu-L-Cys + 3-amino-1-propanol
ADP + phosphate + L-gamma-glutamyl-N-(3-hydroxypropyl)-L-cysteinamide
-
-
-
?
ATP + gamma-L-Glu-L-Cys + 3-amino-1-propanol
ADP + phosphate + L-gamma-glutamyl-N-(3-hydroxypropyl)-L-cysteinamide
-
-
-
?
ATP + gamma-L-Glu-L-Cys + beta-Ala
ADP + phosphate + gamma-Glu-L-Cys-beta-Ala
no activity with L-Ala or D-Ala
-
-
?
ATP + gamma-L-Glu-L-Cys + beta-Ala
ADP + phosphate + gamma-Glu-L-Cys-beta-Ala
-
-
-
-
?
ATP + gamma-L-Glu-L-Cys + beta-Ala
ADP + phosphate + gamma-Glu-L-Cys-beta-Ala
-
-
-
?
ATP + gamma-L-Glu-L-Cys + beta-Ala
ADP + phosphate + gamma-Glu-L-Cys-beta-Ala
-
-
-
?
ATP + gamma-L-Glu-L-Cys + beta-aminoisobutyric acid
ADP + phosphate + gamma-Glu-L-Cys-beta-aminoisobutyric acid
-
-
-
?
ATP + gamma-L-Glu-L-Cys + beta-aminoisobutyric acid
ADP + phosphate + gamma-Glu-L-Cys-beta-aminoisobutyric acid
-
-
-
?
ATP + gamma-L-Glu-L-Cys + D-Ala
ADP + phosphate + gamma-Glu-L-Cys-D-Ala
-
-
-
?
ATP + gamma-L-Glu-L-Cys + D-Ala
ADP + phosphate + gamma-Glu-L-Cys-D-Ala
-
-
-
?
ATP + gamma-L-Glu-L-Cys + D-Ser
ADP + phosphate + gamma-Glu-L-Cys-D-Ser
-
-
-
?
ATP + gamma-L-Glu-L-Cys + D-Ser
ADP + phosphate + gamma-Glu-L-Cys-D-Ser
-
-
-
?
ATP + gamma-L-Glu-L-Cys + ethanolamine
ADP + phosphate + gamma-Glu-L-Cys-ethanolamine
-
-
-
?
ATP + gamma-L-Glu-L-Cys + ethanolamine
ADP + phosphate + gamma-Glu-L-Cys-ethanolamine
-
-
-
?
ATP + gamma-L-Glu-L-Cys + gamma-aminobutyric acid
ADP + phosphate + gamma-Glu-L-Cys-gamma-aminobutyric acid
-
-
-
?
ATP + gamma-L-Glu-L-Cys + gamma-aminobutyric acid
ADP + phosphate + gamma-Glu-L-Cys-gamma-aminobutyric acid
-
-
-
?
ATP + gamma-L-Glu-L-Cys + gamma-aminobutyric acid
ADP + phosphate + gamma-Glu-L-Cys-gamma-aminobutyric acid
-
-
-
?
ATP + gamma-L-Glu-L-Cys + Gly
ADP + phosphate + glutathione
-
-
-
?
ATP + gamma-L-Glu-L-Cys + Gly
ADP + phosphate + glutathione
-
-
-
?
ATP + gamma-L-Glu-L-Cys + Gly
ADP + phosphate + glutathione
-
gamma-glutamyl-cysteine is bound cooperatively by the enzyme, ATP might play a key role in sequential binding, but its amount does not alter the cooperative binding of gamma-glutamyl-cysteine
-
?
ATP + gamma-L-Glu-L-Cys + Gly
ADP + phosphate + glutathione
-
inpresence of dithiothreitol
-
?
ATP + gamma-L-Glu-L-Cys + Gly
ADP + phosphate + glutathione
wild-type enzyme shows negative cooperativity
-
?
ATP + gamma-L-Glu-L-Cys + Gly
ADP + phosphate + glutathione
-
final step of glutathione biosynthesis
-
?
ATP + gamma-L-Glu-L-Cys + Gly
ADP + phosphate + glutathione
second step in the biosynthesis of glutahione
-
?
ATP + gamma-L-Glu-L-Cys + Gly
ADP + phosphate + glutathione
-
-
?
ATP + gamma-L-Glu-L-Cys + Gly
ADP + phosphate + glutathione
-
-
-
?
ATP + gamma-L-Glu-L-Cys + Gly
ADP + phosphate + glutathione
-
ApoE-deficient mice show reduced enzyme expression and activity, genetic regulation mechanism, overview
-
?
ATP + gamma-L-Glu-L-Cys + Gly
ADP + phosphate + glutathione
-
-
-
-
?
ATP + gamma-L-Glu-L-Cys + Gly
ADP + phosphate + glutathione
-
-
-
?
ATP + gamma-L-Glu-L-Cys + Gly
ADP + phosphate + glutathione
-
-
-
?
ATP + gamma-L-Glu-L-Cys + Gly
ADP + phosphate + glutathione
AF333982
-
-
?
ATP + gamma-L-Glu-L-Cys + Gly
ADP + phosphate + glutathione
-
in presence of dithiothreitol
-
?
ATP + gamma-L-Glu-L-Cys + Gly
ADP + phosphate + glutathione
-
wild-type enzyme shows negative cooperativity in binding of gamma-L-Glu-L-Cys
-
r
ATP + gamma-L-Glu-L-Cys + Gly
ADP + phosphate + glutathione
-
second step in the biosynthesis of glutahione
-
r
ATP + gamma-L-Glu-L-Cys + Gly
ADP + phosphate + glutathione
-
-
ir
ATP + gamma-L-Glu-L-Cys + Gly
ADP + phosphate + glutathione
final step in glutathione biosynthesis
-
ir
ATP + gamma-L-Glu-L-Cys + Gly
ADP + phosphate + glutathione
-
-
-
?
ATP + gamma-L-Glu-L-Cys + Gly
ADP + phosphate + glutathione
-
cells are not able to grow without glutathione, wild-type and all mutant enzyme forms can restore activity of the deficient mutant strain on minimal medium without glutathione
-
?
ATP + gamma-L-Glu-L-Cys + Gly
ADP + phosphate + glutathione
-
gene is regulated by stresses via the Atf1-Spc-1-Wis1 signal pathway
-
?
ATP + gamma-L-Glu-L-Cys + Gly
ADP + phosphate + glutathione
-
-
-
-
?
ATP + gamma-L-Glu-L-Cys + Gly
ADP + phosphate + glutathione
-
enzyme catalyzes the final step of glutathione biosynthesis
-
-
?
ATP + gamma-L-Glu-L-Cys + Gly
ADP + phosphate + glutathione
-
-
-
-
?
ATP + gamma-L-Glu-L-Cys + Gly
ADP + phosphate + glutathione
-
-
-
?
ATP + gamma-L-Glu-L-Cys + Gly
ADP + phosphate + glutathione
-
-
-
?
ATP + gamma-L-Glu-L-Cys + L-2,3-diaminopropionic acid
ADP + phosphate + gamma-Glu-L-Cys-L-2,3-diaminopropionic acid
-
-
-
?
ATP + gamma-L-Glu-L-Cys + L-2,3-diaminopropionic acid
ADP + phosphate + gamma-Glu-L-Cys-L-2,3-diaminopropionic acid
-
-
-
?
ATP + gamma-L-Glu-L-Cys + L-2,3-diaminopropionic acid
ADP + phosphate + gamma-Glu-L-Cys-L-2,3-diaminopropionic acid
-
-
-
?
ATP + gamma-L-Glu-L-Cys + L-Ala
ADP + phosphate + gamma-Glu-L-Cys-L-Ala
-
-
-
?
ATP + gamma-L-Glu-L-Cys + L-Ala
ADP + phosphate + gamma-Glu-L-Cys-L-Ala
-
-
-
?
ATP + gamma-L-Glu-L-Cys + L-Orn
ADP + phosphate + gamma-Glu-L-Cys-L-Orn
-
-
-
?
ATP + gamma-L-Glu-L-Cys + L-Orn
ADP + phosphate + gamma-Glu-L-Cys-L-Orn
-
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
-
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
-
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
-
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
-
-
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
-
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
GSH homeostasis in plants is essential for cellular redox control and efficient responses to abiotic and biotic stress. Compartmentation of the GSH biosynthetic pathway is a unique feature of plants, restricting glutathione biosynthesis to the cytosol is sufficient for normal plant development, overview
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
-
-
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
-
an optimally functioning two-step glutathione biosynthetic pathway is required in vivo for a robust defense against arsenite
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
-
-
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
-
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
-
-
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
-
glutathione is a ubiquitous intracellular peptide with diverse functions that include detoxification, antioxidant defense, maintenance of thiol status, and modulation of cell proliferation, whose biosynthesis is tightly regulated, overview. GSH synthase is regulated in a coordinated manner and its up-regulation can further enhance the capacity of the cell to synthesize GSH, enzyme regulation, detailed overview
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
-
-
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
-
glutathione is a ubiquitous intracellular peptide with diverse functions that include detoxification, antioxidant defense, maintenance of thiol status, and modulation of cell proliferation, whose biosynthesis is tightly regulated, overview. GSH synthase is regulated in a coordinated manner and its up-regulation can further enhance the capacity of the cell to synthesize GSH, enzyme regulation, detailed overview. Changes in GSH homeostasis occur in mice with liver-specific retinoid X receptor RXRalpha deletion
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
-
the enzyme catalyzes the last step in glutathione biosynthesis, loss of intracellular neuronal GSH is an important feature of neurodegenerative disorders including Alzheimer's disease, Parkinson's disease, and amyotrophic lateral sclerosis, overview
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
-
-
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
-
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
-
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
-
-
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
-
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
-
glutathione is a ubiquitous intracellular peptide with diverse functions that include detoxification, antioxidant defense, maintenance of thiol status, and modulation of cell proliferation, whose biosynthesis is tightly regulated, overview. GSH synthase is regulated in a coordinated manner and its up-regulation can further enhance the capacity of the cell to synthesize GSH, enzyme regulation, detailed overview
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
the enzyme catalyzes the last step in glutathione biosynthesis
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
-
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
-
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
-
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
-
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
Streptococcus agalactiae serogroup V ATCC BAA-611 / 2603 V/R
-
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
-
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
-
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
-
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
-
-
-
?
dATP + gamma-Glu-L-Cys + Gly
dADP + phosphate + glutathione
-
-
-
-
?
dATP + gamma-Glu-L-Cys + Gly
dADP + phosphate + glutathione
-
75% of the activity relative to ATP
-
-
?
UTP + gamma-Glu-L-Cys + Gly
UDP + phosphate + glutathione
-
10% of the activity relative to ATP
-
-
?
UTP + gamma-Glu-L-Cys + Gly
UDP + phosphate + glutathione
-
10% of the activity relative to ATP
-
-
?
UTP + gamma-Glu-L-Cys + Gly
UDP + phosphate + glutathione
-
24% of the activity relative to ATP
-
-
?
additional information
?
-
-
the loopless mutant shows gamma-Glu-L-Cys-dependent ATP hydrolase activity to almost the same extent as its glutathione synthetase activity
-
-
?
additional information
?
-
-
the loopless mutant shows gamma-Glu-L-Cys-dependent ATP hydrolase activity to almost the same extent as its glutathione synthetase activity
-
-
?
additional information
?
-
-
dysregulation of GSH synthesis occurs in aging and is increasingly being recognized as contributing to the pathogenesis of many pathological conditions including diabetes mellitus, pulmonary fibrosis, cholestatic liver injury, endotoxemia and drug-resistant tumor cells, detailed overview. Decrease in the activity of GS alone without a change in glutathione cysteine ligase, GCL EC 6.3.2.2, and a fall in muscle GSH levels occur after surgical trauma in human skeletal muscle
-
-
?
additional information
?
-
-
dysregulation of GSH synthesis is increasingly being recognized as contributing to the pathogenesis of many pathological conditions including diabetes mellitus, pulmonary fibrosis, cholestatic liver injury, endotoxemia and drug-resistant tumor cells
-
-
?
additional information
?
-
-
glutathione depletion is critical in cardiac dysfunction, antioxidant therapy shows positive effects on the redox state and in the disease, e.g. in metallothionein overexpressing transgenic mice or by application of buthionine sulfoximine, overview
-
-
?
additional information
?
-
-
the anti-oxidant response element promotes the expression of protective proteins including those required for glutathione synthesis, i.e. the xCT cystine antiporter, gamma-glutamylcysteine synthetase and glutathione synthase, overview
-
-
?
additional information
?
-
-
the consequences of GSH depletion include increased oxidative damage to proteins, lipids, and DNA and subsequent cytotoxic effects. GSH is also an important modulator of cellular copper homeostasis and altered Cu metabolism is central to the pathology of several neurodegenerative diseases. Both neurons and fibroblasts revealed increased expression and activation of p53 after depletion of GSH
-
-
?
additional information
?
-
the enzyme forms a disulfide adduct with 2-mercaptoethanol, when purified in the presence of this reducing agent
-
-
?
additional information
?
-
-
the enzyme forms a disulfide adduct with 2-mercaptoethanol, when purified in the presence of this reducing agent
-
-
?
additional information
?
-
assay method development based on [gamma32P]ATP hydrolysis coupled to the GSH synthesis, overview
-
-
?
additional information
?
-
-
assay method development based on [gamma32P]ATP hydrolysis coupled to the GSH synthesis, overview
-
-
?
additional information
?
-
the enzyme forms a disulfide adduct with 2-mercaptoethanol, when purified in the presence of this reducing agent
-
-
?
additional information
?
-
assay method development based on [gamma32P]ATP hydrolysis coupled to the GSH synthesis, overview
-
-
?
additional information
?
-
-
the enzyme catalyzes ADP-ATP exchange at 0.62% of the rate of tripeptide synthesis
-
-
?
additional information
?
-
-
dysregulation of GSH synthesis is increasingly being recognized as contributing to the pathogenesis of many pathological conditions including diabetes mellitus, pulmonary fibrosis, cholestatic liver injury, endotoxemia and drug-resistant tumor cells
-
-
?
additional information
?
-
no activity with beta-alanine and L-serine by wild-type glutathione synthetase
-
-
?
additional information
?
-
-
no activity with beta-alanine and L-serine by wild-type glutathione synthetase
-
-
?
additional information
?
-
the bifunctional enzyme GshF exhibits the activities of glutamate-cyseteine ligase, EC 6.3.2.2, and glutathione synthetase, EC 6.3.2.3
-
-
?
additional information
?
-
the bifunctional enzyme GshF exhibits the activities of glutamate-cyseteine ligase, EC 6.3.2.2, and glutathione synthetase, EC 6.3.2.3
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ATP + gamma-Glu-L-Cys + Gly
?
ATP + gamma-Glu-L-Cys + Gly
ADP + phosphate + gamma-glutathione
ATP + gamma-Glu-L-Cys + Gly
ADP + phosphate + glutathione
ATP + gamma-L-Glu-L-Cys + Gly
ADP + phosphate + glutathione
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
additional information
?
-
ATP + gamma-Glu-L-Cys + Gly
?
-
glutathione biosynthesis
-
-
?
ATP + gamma-Glu-L-Cys + Gly
?
-
-
-
-
?
ATP + gamma-Glu-L-Cys + Gly
?
-
-
-
-
?
ATP + gamma-Glu-L-Cys + Gly
?
-
-
-
-
?
ATP + gamma-Glu-L-Cys + Gly
ADP + phosphate + gamma-glutathione
-
-
ir
ATP + gamma-Glu-L-Cys + Gly
ADP + phosphate + gamma-glutathione
-
-
ir
ATP + gamma-Glu-L-Cys + Gly
ADP + phosphate + gamma-glutathione
-
-
-
ir
ATP + gamma-Glu-L-Cys + Gly
ADP + phosphate + glutathione
-
-
-
ir
ATP + gamma-Glu-L-Cys + Gly
ADP + phosphate + glutathione
-
-
-
ir
ATP + gamma-Glu-L-Cys + Gly
ADP + phosphate + glutathione
patients with hereditary glutathione synthetase deficiency suffer from haemolytic anaemia, 5-oxoprolinuria, metabolic acidosis, recurrent bacterial infections and various degrees of central nervous system dysfunction
-
-
?
ATP + gamma-Glu-L-Cys + Gly
ADP + phosphate + glutathione
two NFE2 sites in the human GSS promoter play important roles in the basal expression of glutathione synthetase. The glutathione synthetase gene expression is also regulated by Nrf2
-
-
?
ATP + gamma-L-Glu-L-Cys + Gly
ADP + phosphate + glutathione
-
-
-
?
ATP + gamma-L-Glu-L-Cys + Gly
ADP + phosphate + glutathione
-
final step of glutathione biosynthesis
-
?
ATP + gamma-L-Glu-L-Cys + Gly
ADP + phosphate + glutathione
second step in the biosynthesis of glutahione
-
?
ATP + gamma-L-Glu-L-Cys + Gly
ADP + phosphate + glutathione
-
-
?
ATP + gamma-L-Glu-L-Cys + Gly
ADP + phosphate + glutathione
-
ApoE-deficient mice show reduced enzyme expression and activity, genetic regulation mechanism, overview
-
?
ATP + gamma-L-Glu-L-Cys + Gly
ADP + phosphate + glutathione
-
-
-
?
ATP + gamma-L-Glu-L-Cys + Gly
ADP + phosphate + glutathione
-
-
-
?
ATP + gamma-L-Glu-L-Cys + Gly
ADP + phosphate + glutathione
AF333982
-
-
?
ATP + gamma-L-Glu-L-Cys + Gly
ADP + phosphate + glutathione
-
second step in the biosynthesis of glutahione
-
r
ATP + gamma-L-Glu-L-Cys + Gly
ADP + phosphate + glutathione
final step in glutathione biosynthesis
-
ir
ATP + gamma-L-Glu-L-Cys + Gly
ADP + phosphate + glutathione
-
gene is regulated by stresses via the Atf1-Spc-1-Wis1 signal pathway
-
?
ATP + gamma-L-Glu-L-Cys + Gly
ADP + phosphate + glutathione
-
enzyme catalyzes the final step of glutathione biosynthesis
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
-
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
-
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
-
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
-
-
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
GSH homeostasis in plants is essential for cellular redox control and efficient responses to abiotic and biotic stress. Compartmentation of the GSH biosynthetic pathway is a unique feature of plants, restricting glutathione biosynthesis to the cytosol is sufficient for normal plant development, overview
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
-
an optimally functioning two-step glutathione biosynthetic pathway is required in vivo for a robust defense against arsenite
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
-
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
-
-
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
-
glutathione is a ubiquitous intracellular peptide with diverse functions that include detoxification, antioxidant defense, maintenance of thiol status, and modulation of cell proliferation, whose biosynthesis is tightly regulated, overview. GSH synthase is regulated in a coordinated manner and its up-regulation can further enhance the capacity of the cell to synthesize GSH, enzyme regulation, detailed overview
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
-
-
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
-
glutathione is a ubiquitous intracellular peptide with diverse functions that include detoxification, antioxidant defense, maintenance of thiol status, and modulation of cell proliferation, whose biosynthesis is tightly regulated, overview. GSH synthase is regulated in a coordinated manner and its up-regulation can further enhance the capacity of the cell to synthesize GSH, enzyme regulation, detailed overview. Changes in GSH homeostasis occur in mice with liver-specific retinoid X receptor RXRalpha deletion
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
-
the enzyme catalyzes the last step in glutathione biosynthesis, loss of intracellular neuronal GSH is an important feature of neurodegenerative disorders including Alzheimer's disease, Parkinson's disease, and amyotrophic lateral sclerosis, overview
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
-
-
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
-
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
-
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
-
glutathione is a ubiquitous intracellular peptide with diverse functions that include detoxification, antioxidant defense, maintenance of thiol status, and modulation of cell proliferation, whose biosynthesis is tightly regulated, overview. GSH synthase is regulated in a coordinated manner and its up-regulation can further enhance the capacity of the cell to synthesize GSH, enzyme regulation, detailed overview
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
the enzyme catalyzes the last step in glutathione biosynthesis
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
-
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
-
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
-
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
-
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
Streptococcus agalactiae serogroup V ATCC BAA-611 / 2603 V/R
-
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
-
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
-
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
-
-
-
?
ATP + gamma-L-glutamyl-L-cysteine + glycine
ADP + phosphate + glutathione
-
-
-
?
additional information
?
-
-
dysregulation of GSH synthesis occurs in aging and is increasingly being recognized as contributing to the pathogenesis of many pathological conditions including diabetes mellitus, pulmonary fibrosis, cholestatic liver injury, endotoxemia and drug-resistant tumor cells, detailed overview. Decrease in the activity of GS alone without a change in glutathione cysteine ligase, GCL EC 6.3.2.2, and a fall in muscle GSH levels occur after surgical trauma in human skeletal muscle
-
-
?
additional information
?
-
-
dysregulation of GSH synthesis is increasingly being recognized as contributing to the pathogenesis of many pathological conditions including diabetes mellitus, pulmonary fibrosis, cholestatic liver injury, endotoxemia and drug-resistant tumor cells
-
-
?
additional information
?
-
-
glutathione depletion is critical in cardiac dysfunction, antioxidant therapy shows positive effects on the redox state and in the disease, e.g. in metallothionein overexpressing transgenic mice or by application of buthionine sulfoximine, overview
-
-
?
additional information
?
-
-
the anti-oxidant response element promotes the expression of protective proteins including those required for glutathione synthesis, i.e. the xCT cystine antiporter, gamma-glutamylcysteine synthetase and glutathione synthase, overview
-
-
?
additional information
?
-
-
the consequences of GSH depletion include increased oxidative damage to proteins, lipids, and DNA and subsequent cytotoxic effects. GSH is also an important modulator of cellular copper homeostasis and altered Cu metabolism is central to the pathology of several neurodegenerative diseases. Both neurons and fibroblasts revealed increased expression and activation of p53 after depletion of GSH
-
-
?
additional information
?
-
the enzyme forms a disulfide adduct with 2-mercaptoethanol, when purified in the presence of this reducing agent
-
-
?
additional information
?
-
-
the enzyme forms a disulfide adduct with 2-mercaptoethanol, when purified in the presence of this reducing agent
-
-
?
additional information
?
-
the enzyme forms a disulfide adduct with 2-mercaptoethanol, when purified in the presence of this reducing agent
-
-
?
additional information
?
-
-
dysregulation of GSH synthesis is increasingly being recognized as contributing to the pathogenesis of many pathological conditions including diabetes mellitus, pulmonary fibrosis, cholestatic liver injury, endotoxemia and drug-resistant tumor cells
-
-
?
additional information
?
-
the bifunctional enzyme GshF exhibits the activities of glutamate-cyseteine ligase, EC 6.3.2.2, and glutathione synthetase, EC 6.3.2.3
-
-
?
additional information
?
-
the bifunctional enzyme GshF exhibits the activities of glutamate-cyseteine ligase, EC 6.3.2.2, and glutathione synthetase, EC 6.3.2.3
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
80
gamma-(alpha-aminomethyl)Glu-2-aminobutyrate
-
-
0.22 - 0.5
gamma-Glu-2-aminobutyrate
0.091
gamma-Glu-L-2-aminobutyrate
-
-
0.03 - 81
gamma-Glu-L-Cys
0.28
gamma-Glu-S-methylcysteine
-
-
0.063
gamma-glutamyl-alpha-aminobutyrate
-
pH 8.2, 37°C
0.1 - 1.6
gamma-L-Glu-aminobutanoate
0.042
gamma-L-Glu-L-alpha-aminobutyrate
-
recombinant enzyme, pH 8.2, 37°C
0.34 - 8.3
gamma-L-Glu-L-Cys
0.099 - 2
gamma-L-glutamyl-L-cysteine
60
N-acetyl-L-2-aminobutyrate
-
-
additional information
additional information
-
0.012
ATP
-
wild-type, 37°C, pH not specified in the publication
0.02
ATP
mutant enzyme Y270H
0.037
ATP
-
recombinant enzyme, pH 8.2, 37°C
0.04
ATP
mutant enzyme D219G
0.05
ATP
mutant enzyme P314L
0.05
ATP
mutant enzyme Y270C
0.057
ATP
wild type enzyme, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
0.07
ATP
wild-type enzyme
0.07
ATP
wild-type enzyme, pH 8.2, 37°C
0.083
ATP
-
reaction with Glu-alpha-aminobutyrate + hydroxylamine
0.089
ATP
mutant enzyme Q226A, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
0.09
ATP
mutant enzyme R283C
0.116
ATP
mutant enzyme S153A, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
0.12
ATP
-
mutant G371V, 37°C, pH not specified in the publication
0.125
ATP
mutant enzyme R132K, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
0.136
ATP
pH 7.5, 25°C, wild-type enzyme
0.17
ATP
pH 7.8, 10°C, recombinant enzyme, ATPase activity
0.171
ATP
mutant enzyme R454K, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
0.175
ATP
mutant enzyme R274K, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
0.18
ATP
mutant enzyme E220A, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
0.18
ATP
pH 7.8, 20°C, recombinant enzyme, ATPase activity
0.18
ATP
pH 7.8, 30°C, recombinant enzyme, ATPase activity
0.189
ATP
mutant enzyme S155A, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
0.19
ATP
mutant enzyme E220Q, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
0.194
ATP
mutant enzyme Q226N, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
0.2 - 1
ATP
pH 7.8, 28°C, recombinant enzyme, ATPase activity
0.24
ATP
-
gamma-Glu-Cys, wild-type enzyme
0.26
ATP
pH 7.8, 15°C, recombinant enzyme, ATPase activity
0.26
ATP
pH 7.8, 30°C, recombinant enzyme, with gamma-L-glutamyl-L-cysteine and glycine
0.28
ATP
pH 7.8, 25°C, recombinant enzyme, ATPase activity
0.299
ATP
pH 8.5, 40°C, recombinant His-tagged enzyme
0.33
ATP
-
pH 8.2, temperature not specified in the publication
0.346
ATP
mutant enzyme E371Q, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
0.356
ATP
pH 8.5, 40°C, recombinant His-tagged enzyme
0.37
ATP
mutant enzyme R454A, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
0.42
ATP
-
wild type enzyme
0.42
ATP
-
inTris-HCl buffer (200 mM, pH 8.2)
0.44
ATP
-
mutant G369V, 37°C, pH not specified in the publication
0.6
ATP
-
mutant with a nicked loop
0.624
ATP
-
mutant enzyme K526A
0.695
ATP
mutant enzyme K456M, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
0.73
ATP
mutant enzyme L188P
0.785
ATP
mutant enzyme N376A, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
0.83
ATP
mutant K305A, pH 8.2, 37°C
1.05
ATP
mutant enzyme D219A
1.54
ATP
-
loopless mutant
2.66
ATP
mutant K305E, pH 8.2, 37°C
4.9
ATP
-
mutant enzyme D448A, in 150 mM Tris-HCl buffer, pH 8.4, 100 mM KCl, 40 mM MgCl2, 0.3 mM EDTA
13.4
ATP
-
mutant enzyme K489A, in 150 mM Tris-HCl buffer, pH 8.4, 100 mM KCl, 40 mM MgCl2, 0.3 mM EDTA
0.32
beta-Ala
pH 8.0, 30°C
0.592
beta-Ala
pH 8.0, 30°C
170
beta-Ala
pH 8.0, 30°C
0.22
gamma-Glu-2-aminobutyrate
-
-
0.5
gamma-Glu-2-aminobutyrate
-
-
0.5
gamma-Glu-2-aminobutyrate
-
ATP
0.2
gamma-Glu-Cys
-
-
0.7
gamma-Glu-Cys
-
loopless mutant
1.87
gamma-Glu-Cys
-
mutant with a nicked loop
0.03
gamma-Glu-L-Cys
pH 8.0, 30°C, with Gly as cosubstrate
0.035
gamma-Glu-L-Cys
mutant enzyme S155A, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
0.039
gamma-Glu-L-Cys
25°C, pH 7.5
0.039
gamma-Glu-L-Cys
wild type enzyme, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
0.06
gamma-Glu-L-Cys
pH 8.0, 30°C, with beta-Ala as cosubstrate
0.1
gamma-Glu-L-Cys
pH 8.0, 30°C, with Gly as cosubstrate
0.129
gamma-Glu-L-Cys
mutant enzyme R132K, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
0.143
gamma-Glu-L-Cys
mutant enzyme R454K, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
0.146
gamma-Glu-L-Cys
mutant enzyme R454A, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
0.166
gamma-Glu-L-Cys
mutant enzyme S153A, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
0.18
gamma-Glu-L-Cys
pH 8.0, 30°C
0.271
gamma-Glu-L-Cys
mutant enzyme N376A, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
0.273
gamma-Glu-L-Cys
mutant enzyme E371Q, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
0.425
gamma-Glu-L-Cys
mutant enzyme K456M, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
0.954
gamma-Glu-L-Cys
mutant enzyme E220Q, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
1.94
gamma-Glu-L-Cys
mutant enzyme E220A, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
3.34
gamma-Glu-L-Cys
mutant enzyme Q226N, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
3.6
gamma-Glu-L-Cys
mutant enzyme Q226A, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
5.9
gamma-Glu-L-Cys
-
inTris-HCl buffer (200 mM, pH 8.2)
5.9
gamma-Glu-L-Cys
-
wild type enzyme, in 150 mM Tris-HCl buffer, pH 8.4, 100 mM KCl, 40 mM MgCl2, 0.3 mM EDTA
7.03
gamma-Glu-L-Cys
mutant enzyme R274K, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
7.5
gamma-Glu-L-Cys
-
mutant enzyme D448A, in 150 mM Tris-HCl buffer, pH 8.4, 100 mM KCl, 40 mM MgCl2, 0.3 mM EDTA
7.5
gamma-Glu-L-Cys
-
mutant enzyme K526A, in 150 mM Tris-HCl buffer, pH 8.4, 100 mM KCl, 40 mM MgCl2, 0.3 mM EDTA
31
gamma-Glu-L-Cys
-
mutant enzyme K489A, in 150 mM Tris-HCl buffer, pH 8.4, 100 mM KCl, 40 mM MgCl2, 0.3 mM EDTA
81
gamma-Glu-L-Cys
-
pH 8.2, 25°C
0.1
gamma-L-Glu-aminobutanoate
-
mutant G371V, 37°C, pH not specified in the publication
0.32
gamma-L-Glu-aminobutanoate
-
mutant V45W, pH 8.2, 37°C
0.89
gamma-L-Glu-aminobutanoate
-
mutant G369V, 37°C, pH not specified in the publication
0.95
gamma-L-Glu-aminobutanoate
-
mutant V44W, pH 8.2, 37°C
1.26
gamma-L-Glu-aminobutanoate
-
wild-type, 37°C, pH not specified in the publication
1.42
gamma-L-Glu-aminobutanoate
-
mutant V44A/V45A, pH 8.2, 37°C
1.42
gamma-L-Glu-aminobutanoate
-
wild-type, pH 8.2, 37°C
1.54
gamma-L-Glu-aminobutanoate
-
mutant V45A, pH 8.2, 37°C
1.6
gamma-L-Glu-aminobutanoate
-
mutant V44A, pH 8.2, 37°C
0.34
gamma-L-Glu-L-Cys
mutant K305A, pH 8.2, 37°C
0.4
gamma-L-Glu-L-Cys
mutant K305E, pH 8.2, 37°C
0.66
gamma-L-Glu-L-Cys
wild-type enzyme, pH 8.2, 37°C
5.9
gamma-L-Glu-L-Cys
-
-
8.3
gamma-L-Glu-L-Cys
-
pH 8.2, 37°C
0.099
gamma-L-glutamyl-L-cysteine
pH 7.5, 25°C, wild-type enzyme
0.1 - 2
gamma-L-glutamyl-L-cysteine
pH 8.2, 37°C, D458N
0.25
gamma-L-glutamyl-L-cysteine
pH 7.8, 30°C, recombinant enzyme
0.25
gamma-L-glutamyl-L-cysteine
pH 8.2, 37°C, D458A
0.29
gamma-L-glutamyl-L-cysteine
pH 8.2, 37°C, D458R
0.762
gamma-L-glutamyl-L-cysteine
-
1.13
gamma-L-glutamyl-L-cysteine
pH 8.5, 40°C, recombinant His-tagged enzyme
1.41
gamma-L-glutamyl-L-cysteine
pH 8.2, 37°C, wild-type enzyme
1.56
gamma-L-glutamyl-L-cysteine
pH 8.5, 40°C, recombinant His-tagged enzyme
0.09
Gly
-
pH 8.2, 25°C
0.53
Gly
-
wild-type, 37°C, pH not specified in the publication
0.91
Gly
-
wild-type enzyme
1.02
Gly
mutant enzyme R283C
1.18
Gly
mutant enzyme E371Q, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
1.24
Gly
mutant enzyme Y270H
1.43
Gly
mutant enzyme Y270C
1.51
Gly
mutant enzyme D219G
1.51
Gly
wild type enzyme, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
1.64
Gly
mutant enzyme P314L
1.67
Gly
mutant enzyme E220Q, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
1.69
Gly
mutant enzyme Q226N, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
1.75
Gly
wild-type enzyme
2.07
Gly
mutant enzyme D219A
2.16
Gly
mutant enzyme R274K, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
2.25
Gly
mutant enzyme L188P
2.25
Gly
mutant enzyme S155A, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
2.4
Gly
mutant enzyme K456M, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
2.52
Gly
-
mutant G371V, 37°C, pH not specified in the publication
3.41
Gly
mutant enzyme S153A, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
3.45
Gly
mutant enzyme Q226A, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
4.04
Gly
mutant enzyme E220A, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
4.17
Gly
mutant enzyme R454K, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
6.3
Gly
-
inTris-HCl buffer (200 mM, pH 8.2)
6.3
Gly
-
wild type enzyme, in 150 mM Tris-HCl buffer, pH 8.4, 100 mM KCl, 40 mM MgCl2, 0.3 mM EDTA
6.59
Gly
mutant enzyme N376A, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
7.57
Gly
mutant enzyme R132K, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
11.8
Gly
-
mutant enzyme K526A, in 150 mM Tris-HCl buffer, pH 8.4, 100 mM KCl, 40 mM MgCl2, 0.3 mM EDTA
16.1
Gly
mutant enzyme R454A, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
23.3
Gly
-
mutant with a nicked loop
23.8
Gly
-
mutant enzyme D448A, in 150 mM Tris-HCl buffer, pH 8.4, 100 mM KCl, 40 mM MgCl2, 0.3 mM EDTA
28
Gly
-
mutant enzyme K489A, in 150 mM Tris-HCl buffer, pH 8.4, 100 mM KCl, 40 mM MgCl2, 0.3 mM EDTA
29.8
Gly
-
loopless mutant
0.07
glycine
pH 8.0, 30°C
0.16
glycine
pH 8.0, 30°C
0.25
glycine
mutant K305A, pH 8.2, 37°C
0.407
glycine
pH 7.5, 25°C, wild-type enzyme
0.452
glycine
-
pH 8.2, 37°C
0.58
glycine
pH 8.2, 37°C, wild-type enzyme
0.75
glycine
pH 7.8, 30°C, recombinant enzyme
0.913
glycine
-
recombinant enzyme, pH 8.2, 37°C
1.3
glycine
pH 8.5, 40°C, recombinant His-tagged enzyme
1.75
glycine
wild-type enzyme, pH 8.2, 37°C
1.96
glycine
mutant K305E, pH 8.2, 37°C
2.1
glycine
pH 8.5, 40°C, recombinant His-tagged enzyme
3 - 5
glycine
pH 8.2, 37°C, D458A
16
glycine
pH 8.2, 37°C, D458N
51
glycine
pH 8.2, 37°C, D458R
additional information
additional information
-
-
-
additional information
additional information
-
-
additional information
additional information
-
-
-
additional information
additional information
-
kinetics
-
additional information
additional information
kinetics
-
additional information
additional information
kinetics
-
additional information
additional information
-
Km-values for Gly and gamma-Glu-Cys are sensitive to the mutation and drastically increased
-
additional information
additional information
-
loopless mutant with increased Km-values, especially for Gly
-
additional information
additional information
-
kinetic measurements
-
additional information
additional information
-
Km-values of wild-type and mutant enzymes
-
additional information
additional information
-
kinetics of cooperative substrate binding
-
additional information
additional information
kinetics, substrate and ligand binding, wild-type enzyme and mutants
-
additional information
additional information
-
kinetics, substrate and ligand binding, wild-type enzyme and mutants
-
additional information
additional information
-
the KM-value for gamma-L-Glu-L-Cys gives a distinctly nonlinear double-reciprocal plot
-
additional information
additional information
steady-state kinetics and kinetic mechanism, overview
-
additional information
additional information
-
steady-state kinetics and kinetic mechanism, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.011 - 55
gamma-Glu-L-Cys
13.6 - 21.7
gamma-L-Glu-aminobutanoate
13
gamma-L-Glu-L-alpha-aminobutyrate
-
recombinant enzyme, pH 8.2, 37°C
0.003 - 6.5
gamma-L-Glu-L-Cys
1.17 - 15.68
gamma-L-glutamyl-L-cysteine
additional information
additional information
-
0.071
ATP
mutant enzyme R132K, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
0.079
ATP
mutant enzyme R454A, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
0.15
ATP
mutant enzyme K456M, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
0.17
ATP
mutant enzyme E371Q, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
0.45
ATP
mutant enzyme R274K, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
0.61
ATP
mutant enzyme N376A, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
0.72
ATP
mutant enzyme Q226A, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
0.87
ATP
pH 7.8, 10°C, recombinant enzyme, ATPase activity
1.46
ATP
mutant enzyme E220A, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
1.593
ATP
mutant enzyme Q226N, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
1.85
ATP
pH 7.8, 15°C, recombinant enzyme, ATPase activity
2.183
ATP
mutant enzyme R454K, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
2.42
ATP
pH 7.8, 20°C, recombinant enzyme, ATPase activity
2.94
ATP
mutant enzyme Q226N, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
2.94
ATP
mutant enzyme R454K, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
3 - 6
ATP
mutant enzyme E220Q, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
3.183
ATP
mutant enzyme E220Q, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
3.3
ATP
mutant enzyme S155A, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
4.72
ATP
pH 7.8, 25°C, recombinant enzyme, ATPase activity
4.99
ATP
pH 7.8, 28°C, recombinant enzyme, ATPase activity
5.083
ATP
mutant enzyme S155A, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
5.32
ATP
pH 7.8, 30°C, recombinant enzyme, ATPase activity
5.4
ATP
pH 7.5, 25°C, wild-type enzyme
5.7
ATP
mutant enzyme S153A, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
12.1
ATP
wild type enzyme, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
13
ATP
-
recombinant enzyme, pH 8.2, 37°C
55
ATP
-
inTris-HCl buffer (200 mM, pH 8.2)
0.011
gamma-Glu-L-Cys
mutant enzyme K456M, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
0.059
gamma-Glu-L-Cys
mutant enzyme R132K, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
0.077
gamma-Glu-L-Cys
mutant enzyme R454A, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
0.158
gamma-Glu-L-Cys
mutant enzyme E371Q, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
0.383
gamma-Glu-L-Cys
mutant enzyme N376A, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
0.842
gamma-Glu-L-Cys
mutant enzyme R274K, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
0.973
gamma-Glu-L-Cys
mutant enzyme Q226A, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
1.485
gamma-Glu-L-Cys
mutant enzyme Q226N, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
1.51
gamma-Glu-L-Cys
mutant enzyme E220A, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
3.13
gamma-Glu-L-Cys
mutant enzyme R454K, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
3.13
gamma-Glu-L-Cys
mutant enzyme S155A, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
3.25
gamma-Glu-L-Cys
mutant enzyme E220Q, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
3.3
gamma-Glu-L-Cys
mutant enzyme S153A, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
3.517
gamma-Glu-L-Cys
mutant enzyme S155A, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
3.817
gamma-Glu-L-Cys
mutant enzyme R454K, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
5.317
gamma-Glu-L-Cys
mutant enzyme S153A, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
6.08
gamma-Glu-L-Cys
mutant enzyme Q226A, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
6.08
gamma-Glu-L-Cys
mutant enzyme Q226N, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
12.2
gamma-Glu-L-Cys
25°C, pH 7.5
12.2
gamma-Glu-L-Cys
wild type enzyme, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
26.9
gamma-Glu-L-Cys
-
pH 8.2, 25°C
55
gamma-Glu-L-Cys
-
inTris-HCl buffer (200 mM, pH 8.2)
13.6
gamma-L-Glu-aminobutanoate
-
mutant V45W, pH 8.2, 37°C
16.4
gamma-L-Glu-aminobutanoate
-
mutant V44W, pH 8.2, 37°C
17.4
gamma-L-Glu-aminobutanoate
-
mutant V45A, pH 8.2, 37°C
18.9
gamma-L-Glu-aminobutanoate
-
mutant V44A, pH 8.2, 37°C
19.5
gamma-L-Glu-aminobutanoate
-
wild-type, pH 8.2, 37°C
21.7
gamma-L-Glu-aminobutanoate
-
mutant V44A/V45A, pH 8.2, 37°C
0.003
gamma-L-Glu-L-Cys
mutant E144K and mutant N146D, pH 8.2, 37°C
0.007
gamma-L-Glu-L-Cys
mutant N146A, pH 8.2, 37°C
0.008
gamma-L-Glu-L-Cys
mutant K364A, pH 8.2, 37°C
0.015
gamma-L-Glu-L-Cys
mutant K364E, pH 8.2, 37°C
0.336
gamma-L-Glu-L-Cys
mutant K305E, pH 8.2, 37°C
0.423
gamma-L-Glu-L-Cys
mutant K305A, pH 8.2, 37°C
6.5
gamma-L-Glu-L-Cys
wild-type enzyme, pH 8.2, 37°C
1.17
gamma-L-glutamyl-L-cysteine
pH 8.2, 37°C, D458R
1.6
gamma-L-glutamyl-L-cysteine
pH 8.2, 37°C, D458A
2.31
gamma-L-glutamyl-L-cysteine
pH 8.2, 37°C, D458N
4.62
gamma-L-glutamyl-L-cysteine
pH 7.5, 25°C, wild-type enzyme
15.68
gamma-L-glutamyl-L-cysteine
pH 8.2, 37°C, wild-type enzyme
0.052
Gly
-
mutant G370V, 37°C, pH not specified in the publication
0.062
Gly
mutant enzyme R132K, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
0.08
Gly
mutant enzyme R454A, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
0.133
Gly
-
mutant G369V, 37°C, pH not specified in the publication
0.157
Gly
mutant enzyme E371Q, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
0.22
Gly
mutant enzyme R274K, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
0.29
Gly
mutant enzyme K456M, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
0.37
Gly
mutant enzyme Q226A, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
1.03
Gly
mutant enzyme N376A, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
1.08
Gly
mutant enzyme E220A, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
1.33
Gly
mutant enzyme Q226N, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
2.36
Gly
-
mutant G371V, 37°C, pH not specified in the publication
2.467
Gly
mutant enzyme R454K, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
2.583
Gly
mutant enzyme E220Q, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
2.94
Gly
mutant enzyme R454K, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
3 - 6
Gly
mutant enzyme E220Q, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
3.3
Gly
mutant enzyme S155A, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
5.183
Gly
mutant enzyme S155A, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
7.2
Gly
mutant enzyme S153A, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
12.6
Gly
wild type enzyme, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase, and 10 units of type II rabbit muscle lactate dehydrogenase
18.8
Gly
-
wild-type, 37°C, pH not specified in the publication
55
Gly
-
inTris-HCl buffer (200 mM, pH 8.2)
1.17
glycine
pH 8.2, 37°C, D458R
1.6
glycine
pH 8.2, 37°C, D458A
2.31
glycine
pH 8.2, 37°C, D458N
4.22
glycine
pH 7.5, 25°C, wild-type enzyme
13
glycine
-
recombinant enzyme, pH 8.2, 37°C
15.68
glycine
pH 8.2, 37°C, wild-type enzyme
additional information
additional information
-
turnover-numbers of wild-type and mutant enzymes
-
additional information
additional information
-
loopless mutant with a 930fold decrease in turnover number
-
additional information
additional information
-
turnover number is fatally reduced in the P227V/G240V mutant
-
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DELTA67-200
-
deletion mutants DELTA67-71 and DELTA67-200 are inactive
DELTA67-71
-
deletion mutants DELTA67-71 and DELTA67-200 are inactive
G374V
-
mutant Lys367/Pro368 to Asn/Ser and mutant Gly374 to Val are inactive
K367N/P368S
-
mutant Lys367/Pro368 to Asn/Ser and mutant Gly374 to Val are inactive
G240V
-
mutant enzymes replaced with Val at the basal position of the flexible loop (P227V, G240V, and P227V/G240V) are identical with wild-type enzyme in their crystal structures, except the loop region
P227V
-
mutant enzymes replaced with Val at the basal position of the flexible loop (P227V, G240V, and P227V/G240V) are identical with wild-type enzyme in their crystal structures, except the loop region
P227V/G240V
-
mutant enzymes replaced with Val at the basal position of the flexible loop (P227V, G240V, and P227V/G240V) are identical with wild-type enzyme in their crystal structures, except the loop region
C294A
-
mutant enzymes Cys294Ala and Cys409Ala retain significant residual activity. Substantial decreases in activity are detected with mutant Cys522Ala and Cys-free mutant Cys294/Cys409/Cys422 to Ala294/Ala409/Ala422
C409A
-
mutant enzymes Cys294Ala and Cys409Ala retain significant residual activity. Substantial decreases in activity are detected with mutant Cys522Ala and Cys-free mutant Cys294/Cys409/Cys422 to Ala294/Ala409/Ala422
C522A
-
mutant enzymes Cys294Ala and Cys409Ala retain significant residual activity. Substantial decreases in activity are detected with mutant Cys522Ala and Cys-free mutant Cys294/Cys409/Cys422 to Ala294/Ala409/Ala422
D219A
naturally occurring missense mutation expressed using a His-tagged, Escherichia coli-based expression system, decreases Vmax to 4% of the wild-type activity
D219G
naturally occurring missense mutation expressed using a His-tagged, Escherichia coli-based expression system, decreases Vmax to 27% of the wild-type activity. Negative cooperativity for L-gamma-glutamyl-L-alpha-aminobutyric acid is changed to positive
D24A
site-directed mutagenesis, the mutant shows a slight increase in catalytic efficiency compared to wild-type enzyme
D458A
site-directed mutagenesis, the mutant shows 10% activity compared to the wild-type enzyme
D458N
site-directed mutagenesis, the mutant shows 15% activity compared to the wild-type enzyme
D458R
site-directed mutagenesis, the mutant shows 7% activity compared to the wild-type enzyme
E144A
site-directed mutagenesis, 0.05% activity compared to the wild-type enzyme, unaltered tertiary structure
E144K
site-directed mutagenesis, inactive mutant, unaltered tertiary structure
G369V
-
mutation in G-loop glycine triad, about 0.7% of wild-type activity. Mutation decreases ligand binding and prevent active site closure and protection
G370V
-
mutation in G-loop glycine triad, about 0.3% of wild-type activity. Mutation decreases ligand binding and prevent active site closure and protection
G371V
-
mutation in G-loop glycine triad, about 13% of wild-type activity
K305A
site-directed mutagenesis, 6.5% activity compared to the wild-type enzyme, 7fold increased Km for glycine, loss of negative cooperativity, 105fold increased Km for ATP, unaltered tertiary structure
K305E
site-directed mutagenesis, 5% activity compared to the wild-type enzyme, loss of negative cooperativity, 40fold increased Km for ATP, unaltered tertiary structure
K364A
site-directed mutagenesis, 0.1% activity compared to the wild-type enzyme, unaltered tertiary structure
K364E
site-directed mutagenesis, 0.2% activity compared to the wild-type enzyme, unaltered tertiary structure
L188P
naturally occurring missense mutation expressed using a His-tagged, Escherichia coli-based expression system, decreases Vmax to 9% of the wild-type activity
N146A
site-directed mutagenesis, 0.1% activity compared to the wild-type enzyme, unaltered tertiary structure
N146D
site-directed mutagenesis, 0.05% activity compared to the wild-type enzyme, unaltered tertiary structure
N146K
site-directed mutagenesis, inactive mutant, unaltered tertiary structure
P314L
naturally occurring neutral mutation
R221A
site-directed mutagenesis, the mutant shows a slight increase in catalytic efficiency compared to wild-type enzyme, the R221A mutation also has a large impact on the intrachain bonding structure
R283C
naturally occurring missense mutation expressed using a His-tagged, Escherichia coli-based expression system, decreases Vmax to 13% of the wild-type activity
S42A
site-directed mutagenesis, the mutant shows a slight increase in catalytic efficiency compared to wild-type enzyme
V44A
-
decrease in melting temperature, slight decrease in activity
V44A/V45A
-
decrease in melting temperature, initial activity similar to wild-type
V44W
-
decrease in melting temperature, 16% decrease in activity
V45A
-
decrease in melting temperature, slight decrease in activity
V45W
-
decrease in melting temperature, 30% decrease in activity
Y208C
naturally occurring missense mutation expressed using a His-tagged, Escherichia coli-based expression system, decreases Vmax to 2% of the wild-type activity
Y270H
naturally occurring missense mutation expressed using a His-tagged, Escherichia coli-based expression system, decreases Vmax to 6% of the wild-type activity
A485L/T486P
site-directed mutagenesis, the mutant shows 70% reduced activity compared to the wild-type activity, and a shift of substrate specificity with increased affinity of GSH2 for Ser as a substrate, while affinity to Gly is preserved. This provides another biosynthetic pathway for hydroxymethyl glutathione, which is known to be synthesized from glutathione and Ser in a reaction catalysed by carboxypeptidase Y
I471M/C472M/A485L/T486P
site-directed mutagenesis, the mutant shows 38% reduced activity compared to the wild-type activity, and a shift of substrate specificity with 1.2fold increased affinity of GSH2 for beta-Ala and lowered affinity for Gly, which is a characteristic of the enzyme homoglutathione synthetase found in plants, EC 6.3.2.23
I471M/C472V
site-directed mutagenesis, the mutant shows showed much lower affinity towards Gly and 78% reduced activity compared to the wild-type activity, but no other differences
H144A
-
higher activity than the wild type enzyme
K485A
-
very low activity
K526A
-
very low activity
E429A
inactive enzyme
E429Q
inactive enzyme
additional information
construction of gsh2 insertion mutants, the mutants have a seedling lethal phenotype in contrast to the embryo lethal phenotype of gamma-glutamate cysteine ligase, gsh1, EC 6.3.2.2, null mutants, overview. The mutants show hyperaccumulation of gamma-glutamylcysteine to levels 5000-fold that in the wild-type and 200fold wild-type levels of GSH, phenotype, overview. Complementation of gsh2 mutants with the cytosol-specific GSH2 give rise to phenotypically wild-type transgenic plants
additional information
-
construction of transgenic plants by overexpression of the Escherichia coli enzyme, encoded by gene gshII, in the cytosol of transgenic plants, the plants show 3fold increased ability in the shoot compared to the wild-type to accumulate and tolerate heavy metals, e.g. cadmium
additional information
-
creation of targeted X chromosomal deficiency lines. Relative arsenite sensitivity arises when the dose of the glutathione synthetase gene expression is reduced by half. Knockdown of GS expression by RNAi in cultured S2 cells leads to enhanced arsenite sensitivity, while GS RNAi applied to intact organisms dramatically reduces the concentration of food-borne arsenite compatible with successful growth and development, phenotypes, overview
additional information
-
deletion mutant of the loop and mutant with a nicked multifunctional loop. Cleavage of the loop results in a drastic increase in activity, which is similar to the results for the loop deletion. High concentrations of ATP inhibit the wild-type enzyme, while both nicked and loopless enzyme are not inhibited
additional information
-
the mutant enzymes Arg86 and Asn283 are altered in their kinetic parameters, especially the Michaelis constant of gamma-Glu-Cys
additional information
-
the crystal structure of the loopless mutant, in which the loop is replaced by 3 Gly residues, is identical with that of the wild-type enzyme. Replacement of the loop increases the Km-values, especially for glycine, and a 930fold decrease in turnover number. The loopless mutant shows gamma-Glu-L-Cys-dependent ATP hydrolase activity to almost the same extent as its glutathione synthetase activity
additional information
-
construction of transgenic plants by overexpression of the enzyme in the cytosol of Brassica juncea, i.e. Indian mustard, transgenic plants show 3fold increased ability in the shoot compared to the wild-type to accumulate and tolerate heavy metals, e.g. cadmium, for use in detoxification
additional information
-
the mutant enzymes Arg86 and Asn283 are altered in their kinetic parameters, especially the Michaelis constant of gamma-Glu-Cys
-
additional information
-
the crystal structure of the loopless mutant, in which the loop is replaced by 3 Gly residues, is identical with that of the wild-type enzyme. Replacement of the loop increases the Km-values, especially for glycine, and a 930fold decrease in turnover number. The loopless mutant shows gamma-Glu-L-Cys-dependent ATP hydrolase activity to almost the same extent as its glutathione synthetase activity
-
additional information
all Asp458 mutants display a change in cooperativity from negative cooperativity to non-cooperative. All mutants show similar stability as compared to wild-type enzyme, differential scanning calorimetry
additional information
-
all Asp458 mutants display a change in cooperativity from negative cooperativity to non-cooperative. All mutants show similar stability as compared to wild-type enzyme, differential scanning calorimetry
additional information
structure and stability comparisons of wild-type enzyme and mutant enzymes, overview
additional information
-
structure and stability comparisons of wild-type enzyme and mutant enzymes, overview
additional information
-
ApoE-deficient mice show reduced enzyme expression and activity
additional information
-
decreased hepatic GSH levels occur, which correlated with a fall in GS activity, in Tat transgenic mice. GCLC and GS are coordinately regulated but GCLM is unchanged in liver-specific retinoid X receptor alpha knockout mice
additional information
deletion of genes GSH1 and GSH2 (encoding glutathione synthetase) using the CRISPR-Cas9 nuclease system
additional information
-
deletion of genes GSH1 and GSH2 (encoding glutathione synthetase) using the CRISPR-Cas9 nuclease system
additional information
generation of an GSH2 enzyme deletion mutant using the CRISPR-Cas9 nuclease system
additional information
-
generation of an GSH2 enzyme deletion mutant using the CRISPR-Cas9 nuclease system
additional information
-
deletion of genes GSH1 and GSH2 (encoding glutathione synthetase) using the CRISPR-Cas9 nuclease system
-
additional information
-
generation of an GSH2 enzyme deletion mutant using the CRISPR-Cas9 nuclease system
-
additional information
-
elimination of the protease cleavage site in the 56 kDa subunit by site-directed mutagenesis results in expression of a stable and functional enzyme
additional information
enzymatic production of glutathione by recombinant cell-free bifunctional gamma-glutamylcysteine synthetase/glutathione synthetase (gamma-GCS-GS or GshF) coupled with in vitro acetate kinase-based ATP generation in Escherichia coli strain Rosetta (DE3), method optimization. The recombinant enzyme comprises both the activities of gamma-glutamylcysteine synthetase (gamma-GCS or GSHI, EC 6.3.2.2) and GSH synthetase (GS or GSHII, EC 6.3.2.3). The gshF from Streptomyces thermophilus shows poor expression levels compared to gshF from Streptomyces agalactiae. GSH production resulting from a combination of recombinant Escherichia coli BL21(DE3) expressing gshF from Streptomyces agalactiae with recombinant Escherichia coli BL21(DE3) expressing acetate kinase from Lactobacillus sanfranciscensis is 2.5 times higher than that of gshF from Streptomyces thermophilus
additional information
Streptococcus agalactiae serogroup V ATCC BAA-611 / 2603 V/R
-
enzymatic production of glutathione by recombinant cell-free bifunctional gamma-glutamylcysteine synthetase/glutathione synthetase (gamma-GCS-GS or GshF) coupled with in vitro acetate kinase-based ATP generation in Escherichia coli strain Rosetta (DE3), method optimization. The recombinant enzyme comprises both the activities of gamma-glutamylcysteine synthetase (gamma-GCS or GSHI, EC 6.3.2.2) and GSH synthetase (GS or GSHII, EC 6.3.2.3). The gshF from Streptomyces thermophilus shows poor expression levels compared to gshF from Streptomyces agalactiae. GSH production resulting from a combination of recombinant Escherichia coli BL21(DE3) expressing gshF from Streptomyces agalactiae with recombinant Escherichia coli BL21(DE3) expressing acetate kinase from Lactobacillus sanfranciscensis is 2.5 times higher than that of gshF from Streptomyces thermophilus
-
additional information
a recombinant Escherichia coli strain expressing gshF encoding the bifunctional glutathione synthetase of Streptococcus thermophilus is constructed for efficient GSH production. The cultivation process is optimized by controlling dissolved oxygen, amino acid addition, and glucose feeding. 36.8 mM (11.3 g/l) GSH are formed at a productivity of 2.06 mM/h when the amino acid precursors (75 mM each) are added and glucose is supplied as the sole carbon and energy source. The fed-batch fermentations are performed in a 5-l bioreactor containing 2.5 l medium for fed-batch culture inoculated with 140 ml secondary seed culture. The temperature and pH are controlled at 37°C and 7.0, respectively. The GSH production is extremely limited by the precursors of GSH, and the GSH productivity is only 0.18 mM/h. Method evaluation, overview
additional information
enzymatic production of glutathione by recombinant cell-free bifunctional gamma-glutamylcysteine synthetase/glutathione synthetase (gamma-GCS-GS or GshF) coupled with in vitro acetate kinase-based ATP generation in Escherichia coli strain Rosetta (DE3), method optimization. The recombinant enzyme comprises both the activities of gamma-glutamylcysteine synthetase (gamma-GCS or GSHI, EC 6.3.2.2) and GSH synthetase (GS or GSHII, EC 6.3.2.3). The gshF from Streptomyces thermophilus shows poor expression levels compared to gshF from Streptomyces agalactiae. GSH production resulting from a combination of recombinant Escherichia coli BL21(DE3) expressing gshF from Streptomyces agalactiae with recombinant Escherichia coli BL21(DE3) expressing acetate kinase from Lactobacillus sanfranciscensis is 2.5 times higher than that of gshF from Streptomyces thermophilus with acetate kinase from Escherichia coli
additional information
-
enzymatic production of glutathione by recombinant cell-free bifunctional gamma-glutamylcysteine synthetase/glutathione synthetase (gamma-GCS-GS or GshF) coupled with in vitro acetate kinase-based ATP generation in Escherichia coli strain Rosetta (DE3), method optimization. The recombinant enzyme comprises both the activities of gamma-glutamylcysteine synthetase (gamma-GCS or GSHI, EC 6.3.2.2) and GSH synthetase (GS or GSHII, EC 6.3.2.3). The gshF from Streptomyces thermophilus shows poor expression levels compared to gshF from Streptomyces agalactiae. GSH production resulting from a combination of recombinant Escherichia coli BL21(DE3) expressing gshF from Streptomyces agalactiae with recombinant Escherichia coli BL21(DE3) expressing acetate kinase from Lactobacillus sanfranciscensis is 2.5 times higher than that of gshF from Streptomyces thermophilus with acetate kinase from Escherichia coli
additional information
to convert feather hydrolysates into GSH with high values, the bifunctional glutathione synthetase, that comprises the activities of EC 6.3.2.2 and EC 6.3.2.3, encoded by gcsgs from Streptococcus thermophilus is surface displayed on Saccharomyces cerevisiae strain EBY100, the potential in glutathione (GSH) production from feather hydrolysates is analyzed. The surface-displayed GCSGS can be used to convert feather hydrolysates into GSH. 10 g/l of feather are converted into 321.8 mg/l GSH by the Trichoderma atroviride F6, with feather degrading ability, and surface-displayed GCSGS. Method optimization, overview
additional information
-
enzymatic production of glutathione by recombinant cell-free bifunctional gamma-glutamylcysteine synthetase/glutathione synthetase (gamma-GCS-GS or GshF) coupled with in vitro acetate kinase-based ATP generation in Escherichia coli strain Rosetta (DE3), method optimization. The recombinant enzyme comprises both the activities of gamma-glutamylcysteine synthetase (gamma-GCS or GSHI, EC 6.3.2.2) and GSH synthetase (GS or GSHII, EC 6.3.2.3). The gshF from Streptomyces thermophilus shows poor expression levels compared to gshF from Streptomyces agalactiae. GSH production resulting from a combination of recombinant Escherichia coli BL21(DE3) expressing gshF from Streptomyces agalactiae with recombinant Escherichia coli BL21(DE3) expressing acetate kinase from Lactobacillus sanfranciscensis is 2.5 times higher than that of gshF from Streptomyces thermophilus with acetate kinase from Escherichia coli
-
additional information
-
a recombinant Escherichia coli strain expressing gshF encoding the bifunctional glutathione synthetase of Streptococcus thermophilus is constructed for efficient GSH production. The cultivation process is optimized by controlling dissolved oxygen, amino acid addition, and glucose feeding. 36.8 mM (11.3 g/l) GSH are formed at a productivity of 2.06 mM/h when the amino acid precursors (75 mM each) are added and glucose is supplied as the sole carbon and energy source. The fed-batch fermentations are performed in a 5-l bioreactor containing 2.5 l medium for fed-batch culture inoculated with 140 ml secondary seed culture. The temperature and pH are controlled at 37°C and 7.0, respectively. The GSH production is extremely limited by the precursors of GSH, and the GSH productivity is only 0.18 mM/h. Method evaluation, overview
-
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Mus musculus
brenda
Du, T.; Ciccotosto, G.D.; Cranston, G.A.; Kocak, G.; Masters, C.L.; Crouch, P.J.; Cappai, R.; White, A.R.
Neurotoxicity from glutathione depletion is mediated by Cu-dependent p53 activation
Free Radic. Biol. Med.
44
44-55
2008
Mus musculus
brenda
Bahia, P.K.; Rattray, M.; Williams, R.J.
Dietary flavonoid (-)epicatechin stimulates phosphatidylinositol 3-kinase-dependent anti-oxidant response element activity and up-regulates glutathione in cortical astrocytes
J. Neurochem.
106
2194-2204
2008
Mus musculus
brenda
Lu, S.C.
Regulation of glutathione synthesis
Mol. Aspects Med.
30
42-59
2008
Homo sapiens, Mus musculus, Rattus norvegicus
brenda
Pasternak, M.; Lim, B.; Wirtz, M.; Hell, R.; Cobbett, C.S.; Meyer, A.J.
Restricting glutathione biosynthesis to the cytosol is sufficient for normal plant development
Plant J.
53
999-1012
2008
Arabidopsis thaliana (P46416)
brenda
Nishiya, T.; Mori, K.; Hattori, C.; Kai, K.; Kataoka, H.; Masubuchi, N.; Jindo, T.; Manabe, S.
The crucial protective role of glutathione against tienilic acid hepatotoxicity in rats
Toxicol. Appl. Pharmacol.
232
280-291
2008
Rattus norvegicus (P46413)
brenda
Muniz Ortiz, J.G.; Opoka, R.; Kane, D.; Cartwright, I.L.
Investigating arsenic susceptibility from a genetic perspective in Drosophila reveals a key role for glutathione synthetase
Toxicol. Sci.
107
416-426
2008
Drosophila melanogaster
brenda
Jackson, R.M.; Gupta, C.
Hypoxia and kinase activity regulate lung epithelial cell glutathione
Exp. Lung Res.
36
45-56
2010
Homo sapiens
brenda
Cruz de Carvalho, M.H.; Brunet, J.; Bazin, J.; Kranner, I.; d Arcy-Lameta, A.; Zuily-Fodil, Y.; Contour-Ansel, D.
Homoglutathione synthetase and glutathione synthetase in drought-stressed cowpea leaves: expression patterns and accumulation of low-molecular-weight thiols
J. Plant Physiol.
167
480-487
2010
Vigna unguiculata
brenda
Fyfe, P.K.; Alphey, M.S.; Hunter, W.N.
Structure of Trypanosoma brucei glutathione synthetase: domain and loop alterations in the catalytic cycle of a highly conserved enzyme
Mol. Biochem. Parasitol.
170
93-99
2010
Trypanosoma brucei
brenda
Uchida, M.; Sugaya, M.; Kanamaru, T.; Hisatomi, H.
Alternative RNA splicing in expression of the glutathione synthetase gene in human cells
Mol. Biol. Rep.
37
2105-2109
2010
Homo sapiens (P48637), Homo sapiens
brenda
Liedschulte, V.; Wachter, A.; Zhigang, A.; Rausch, T.
Exploiting plants for glutathione (GSH) production: Uncoupling GSH synthesis from cellular controls results in unprecedented GSH accumulation
Plant Biotechnol. J.
8
1-14
2010
Streptococcus thermophilus (D7P1H2)
brenda
Dinescu, A.; Brown, T.R.; Barelier, S.; Cundari, T.R.; Anderson, M.E.
The role of the glycine triad in human glutathione synthetase
Biochem. Biophys. Res. Commun.
400
511-516
2010
Homo sapiens
brenda
Slavens, K.D.; Brown, T.R.; Barakat, K.A.; Cundari, T.R.; Anderson, M.E.
Valine 44 and valine 45 of human glutathione synthetase are key for subunit stability and negative cooperativity
Biochem. Biophys. Res. Commun.
410
597-601
2011
Homo sapiens
brenda
Li, W.; Li, Z.; Yang, J.; Ye, Q.
Production of glutathione using a bifunctional enzyme encoded by gshF from Streptococcus thermophilus expressed in Escherichia coli
J. Biotechnol.
154
261-268
2011
Streptococcus thermophilus (D4N891), Streptococcus thermophilus SIIM B218 (D4N891)
brenda
Sharma, S.K.; Banyal, H.S.
Characterization of Plasmodium berghei glutathione synthetase
Parasitol. Int.
60
321-323
2011
Plasmodium berghei
brenda
Cameron, J.C.; Pakrasi, H.B.
Essential role of glutathione in acclimation to environmental and redox perturbations in the cyanobacterium Synechocystis sp. PCC 6803
Plant Physiol.
154
1672-1685
2010
Synechocystis sp. (P73493), Synechocystis sp.
brenda
Brown, T.R.; Drummond, M.L.; Barelier, S.; Crutchfield, A.S.; Dinescu, A.; Slavens, K.D.; Cundari, T.R.; Anderson, M.E.
Aspartate 458 of human glutathione synthetase is important for cooperativity and active site structure
Biochem. Biophys. Res. Commun.
411
536-542
2011
Homo sapiens (P48637), Homo sapiens
brenda
Musgrave, W.B.; Yi, H.; Kline, D.; Cameron, J.C.; Wignes, J.; Dey, S.; Pakrasi, H.B.; Jez, J.M.
Probing the origins of glutathione biosynthesis through biochemical analysis of glutamate-cysteine ligase and glutathione synthetase from a model photosynthetic prokaryote
Biochem. J.
450
63-72
2013
Synechocystis sp. (P73493), Synechocystis sp.
brenda
Merlino, A.; Russo Krauss, I.; Albino, A.; Pica, A.; Vergara, A.; Masullo, M.; De Vendittis, E.; Sica, F.
Improving protein crystal quality by the without-oil microbatch method: crystallization and preliminary X-ray diffraction analysis of glutathione synthetase from Pseudoalteromonas haloplanktis
Int. J. Mol. Sci.
12
6312-6319
2011
Pseudoalteromonas haloplanktis
brenda
Albino, A.; Marco, S.; Di Maro, A.; Chambery, A.; Masullo, M.; De Vendittis, E.
Characterization of a cold-adapted glutathione synthetase from the psychrophile Pseudoalteromonas haloplanktis
Mol. Biosyst.
8
2405-2414
2012
Pseudoalteromonas haloplanktis (Q3IFA2), Pseudoalteromonas haloplanktis, Pseudoalteromonas haloplanktis TAC 125 (Q3IFA2)
brenda
Dworeck, T.; Zimmermann, M.
Site directed mutagenesis of Schizosaccharomyces pombe glutathione synthetase produces an enzyme with homoglutathione synthetase activity
PLoS ONE
7
e46580
2012
Schizosaccharomyces pombe (P35669), Schizosaccharomyces pombe
brenda
Grabek-Lejko, D.; Kurylenko, O.O.; Sibirny, V.A.; Ubiyvovk, V.M.; Penninckx, M.; Sibirny, A.A.
Alcoholic fermentation by wild-type Hansenula polymorpha and Saccharomyces cerevisiae versus recombinant strains with an elevated level of intracellular glutathione
J. Ind. Microbiol. Biotechnol.
38
1853-1859
2011
Ogataea angusta (A0A067XH95)
brenda
Jiang, Y.; Tao, R.; Shen, Z.; Sun, L.; Zhu, F.; Yang, S.
Enzymatic production of glutathione by bifunctional gamma-glutamylcysteine synthetase/glutathione synthetase coupled with in vitro acetate kinase-based ATP generation
Appl. Biochem. Biotechnol.
180
1446-1455
2016
Streptococcus thermophilus (D4N891), Streptococcus thermophilus, Streptococcus agalactiae serogroup V (Q8DXM9), Streptococcus agalactiae serogroup V ATCC BAA-611 / 2603 V/R (Q8DXM9), Streptococcus thermophilus SIIM B218 (D4N891)
brenda
Yang, J.; Li, W.; Wang, D.; Wu, H.; Li, Z.; Ye, Q.
Characterization of bifunctional L-glutathione synthetases from Actinobacillus pleuropneumoniae and Actinobacillus succinogenes for efficient glutathione biosynthesis
Appl. Microbiol. Biotechnol.
100
6279-6289
2016
Actinobacillus succinogenes (A6VQP8), Actinobacillus pleuropneumoniae (D4N892), Actinobacillus pleuropneumoniae ATCC 55618 (D4N892)
brenda
Qiu, Z.; Deng, Z.; Tan, H.; Zhou, S.; Cao, L.
Engineering the robustness of Saccharomyces cerevisiae by introducing bifunctional glutathione synthase gene
J. Ind. Microbiol. Biotechnol.
42
537-542
2015
Streptococcus thermophilus (D7P1H2)
brenda
Wang, D.; Wang, C.; Wu, H.; Li, Z.; Ye, Q.
Glutathione production by recombinant Escherichia coli expressing bifunctional glutathione synthetase
J. Ind. Microbiol. Biotechnol.
43
45-53
2016
Streptococcus thermophilus (D4N891), Streptococcus thermophilus SIIM B218 (D4N891)
brenda
Qiu, Z.; Tan, H.; Zhou, S.; Cao, L.
Surface display of a bifunctional glutathione synthetase on Saccharomyces cerevisiae for converting chicken feather hydrolysate into glutathione
Mol. Biotechnol.
56
726-730
2014
Streptococcus thermophilus (D7P1H2)
brenda
Kong, M.; Wang, F.; Tian, L.; Tang, H.; Zhang, L.
Functional identification of glutamate cysteine ligase and glutathione synthetase in the marine yeast Rhodosporidium diobovatum
Naturwissenschaften
105
doi: 10.1007/s00114-017-1520-2
2017
Rhodotorula diobovata (A0A0U3DG08), Rhodotorula diobovata, Rhodotorula diobovata MCCC 2A00023 (A0A0U3DG08)
brenda
De Jesus, M.C.; Ingle, B.L.; Barakat, K.A.; Shrestha, B.; Slavens, K.D.; Cundari, T.R.; Anderson, M.E.
The role of strong electrostatic interactions at the dimer interface of human glutathione synthetase
Protein J.
33
403-409
2014
Homo sapiens (P48637), Homo sapiens
brenda