The Enzyme Database

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Accepted name: L-glutamate—[L-glutamyl-carrier protein] ligase
Reaction: ATP + L-glutamate + holo-[L-glutamyl-carrier protein] = AMP + diphosphate + L-glutamyl-[L-glutamyl-carrier protein] (overall reaction)
(1a) ATP + L-glutamate = diphosphate + (L-glutamyl)adenylate
(1b) (L-glutamyl)adenylate + holo-[L-glutamyl-carrier protein] = AMP + L-glutamyl-[L-glutamyl-carrier protein]
Other name(s): ambE (gene name)
Systematic name: L-glutamate:[L-glutamyl-carrier protein] ligase (AMP-forming)
Comments: The adenylation domain of the enzyme catalyses the activation of L-glutamate to (L-glutamyl)adenylate, followed by the transfer of the activated compound to the free thiol of a phosphopantetheine arm of a peptidyl-carrier protein domain. The peptidyl-carrier protein domain may be part of the same protein, or of a different protein. This activity is often found as part of a larger non-ribosomal peptide synthase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
1.  Rojas Murcia, N., Lee, X., Waridel, P., Maspoli, A., Imker, H.J., Chai, T., Walsh, C.T. and Reimmann, C. The Pseudomonas aeruginosa antimetabolite L -2-amino-4-methoxy-trans-3-butenoic acid (AMB) is made from glutamate and two alanine residues via a thiotemplate-linked tripeptide precursor. Front. Microbiol. 6:170 (2015). [DOI] [PMID: 25814981]
[EC created 2021]

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