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Literature summary for 6.3.2.2 extracted from

  • Katoh, M.; Hiratake, J.; Oda, J.i.
    ATP-dependent inactivation of Escherichia coli gamma-glutamylcysteine synthetase by L-glutamic acid gamma-monohydroxamate (1998), Biosci. Biotechnol. Biochem., 62, 1455-1457.
    View publication on PubMed
Search for more literature for 6.3.2.2

Inhibitors

Inhibitors Comment Organism Structure
L-glutamic acid gamma-monohydroxamate ATP-dependent irreversible inactivation, loss of 90% activity within 3 days, inactivation mechanism, no inactivation occurs in absence of ATP or with AMP-PNP Escherichia coli
additional information no inacivationwith ATP alone or with L-aspartic acid gamma-monohydroxamate Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + L-Glu + L-Cys Escherichia coli first and rate-limiting step in the biosynthesis of glutathione ADP + phosphate + gamma-L-Glu-L-Cys
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Reaction

Reaction Comment Organism Reaction ID
ATP + L-glutamate + L-cysteine = ADP + phosphate + gamma-L-glutamyl-L-cysteine reaction mechanism Escherichia coli
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-Glu + L-Cys
-
 Escherichia coli ADP + phosphate + gamma-L-Glu-L-Cys
-
 ?
ATP + L-Glu + L-Cys first and rate-limiting step in the biosynthesis of glutathione Escherichia coli ADP + phosphate + gamma-L-Glu-L-Cys
-
 ?

Synonyms

Synonyms Comment Organism
gamma-GCS
-
 Escherichia coli
gamma-Glutamylcysteine synthetase
-
 Escherichia coli

Cofactor

Cofactor Comment Organism Structure
ATP dependent on Escherichia coli