The Enzyme Database

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Accepted name: glyine—[glycyl-carrier protein] ligase
Reaction: ATP + glycine + holo-[glycyl-carrier protein] = AMP + diphosphate + glycyl-[glycyl-carrier protein] (overall reaction)
(1a) ATP + glycine = diphosphate + (glycyl)adenylate
(1b) (glycyl)adenylate + holo-[glycyl-carrier protein] = AMP + glycyl-[glycyl-carrier protein]
Other name(s): dhbF (gene name); sfmB (gene name)
Systematic name: glycine:[glycyl-carrier protein] ligase (AMP-forming)
Comments: The adenylation domain of the enzyme catalyses the activation of glycine to (glycyl)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 (as in the case of DhbF in bacillibactin biosynthesis), 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
1.  May, J.J., Wendrich, T.M. and Marahiel, M.A. The dhb operon of Bacillus subtilis encodes the biosynthetic template for the catecholic siderophore 2,3-dihydroxybenzoate-glycine-threonine trimeric ester bacillibactin. J. Biol. Chem. 276 (2001) 7209–7217. [DOI] [PMID: 11112781]
2.  Li, L., Deng, W., Song, J., Ding, W., Zhao, Q.F., Peng, C., Song, W.W., Tang, G.L. and Liu, W. Characterization of the saframycin A gene cluster from Streptomyces lavendulae NRRL 11002 revealing a nonribosomal peptide synthetase system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. J. Bacteriol. 190 (2008) 251–263. [DOI] [PMID: 17981978]
[EC created 2021]

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