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Literature summary extracted from

  • Rhee, S.G.; Chock, P.B.; Stadtman, E.R.
    Glutamine synthetase from Escherichia coli (1985), Methods Enzymol., 113, 213-241.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
6.3.1.2 AMP
-
 Escherichia coli
6.3.1.2 Carbamoyl-phosphoalanine
-
 Escherichia coli
6.3.1.2 CTP
-
 Escherichia coli
6.3.1.2 glucosamine 6-phosphate
-
 Escherichia coli
6.3.1.2 Gly
-
 Escherichia coli
6.3.1.2 Ser
-
 Escherichia coli
6.3.1.2 Trp
-
 Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
6.3.1.2 additional information
-
 additional information the enzyme is modulated by a closed bicyclic covalent interconvertible cascade. It consists of two protein nucleotidylation cycles. One involves the cyclic adenylylation and deadenylylation of glutamine synthetase, the other involves the uridylylation and deuridylylation of Shapiro´s regulatory protein PII Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
6.3.1.2 ATP + L-Glu + NH4+ Escherichia coli glutamine produced by the enzyme serves as a source of nitrogen atoms in the biosynthesis of all amino acids, purine and pyrimidine nucleotides, of glucosamine 6-phosphate, 4-aminobenzoic acid, and of nicotinamide derivatives. Glutamine synthetase links the assimilation of NH4+ with biosynthetic pathways leading to the formation of proteins, nucleic acids, complex polysaccharides, and different coenzymes ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
6.3.1.2 Escherichia coli
-
 wild-type and site-directed mutants H4A, H4C, M8L, H12L, H12D
-

Oxidation Stability

EC Number Oxidation Stability Organism
6.3.1.2 oxidation inactivation catalyzed by mixed function oxidation systems requires the presence of O2, and in general, is stimulated by Fe3+ and is inhibited by catalase, by metal ion chelating agents, and by Mn2+. In addition several nonenzymatic oxidation systems, namely 1. ascorbate, Fe3+ and O2 2. Fe2+ and H2O2 or O2 3. dihydroxyfumarate, Fe2+ and O2 are also found to cause inactivation Escherichia coli

Purification (Commentary)

EC Number Purification (Comment) Organism
6.3.1.2 purification methods Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.3.1.2 ATP + L-Glu + NH4+
-
 Escherichia coli ADP + phosphate + L-Gln
-
 ?
6.3.1.2 ATP + L-Glu + NH4+ glutamine produced by the enzyme serves as a source of nitrogen atoms in the biosynthesis of all amino acids, purine and pyrimidine nucleotides, of glucosamine 6-phosphate, 4-aminobenzoic acid, and of nicotinamide derivatives. Glutamine synthetase links the assimilation of NH4+ with biosynthetic pathways leading to the formation of proteins, nucleic acids, complex polysaccharides, and different coenzymes Escherichia coli ?
-
 ?