1995
DOI: 10.1021/bi00014a017
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Gramicidin S synthetase 1 (phenylalanine racemase), a prototype of amino acid racemases containing the cofactor 4'-phosphopantetheine

Abstract: The biosynthesis of the decapeptide antibiotic gramicidin S in Bacillus brevis ATCC 9999 is catalyzed by a multienzyme system consisting of two multifunctional proteins, gramicidin S synthetase 1 and 2, encoded by the grsA and grsB genes, respectively. Gramicidin S synthetase 1 (phenylalanine racemase, EC 5.1.1.11, GS1) racemizes phenylalanine in the thioester-bound stage. The amount of 4'-phosphopantetheine liberated from highly purified GS1 was determined microbiologically using Lacto-bacillus plantarum as t… Show more

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Cited by 71 publications
(53 citation statements)
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“…The disrupted phbH gene of NS414 encodes a PCP-containing thiolation domain. Covalent modification of PCPs with a 4Ј-phosphopantetheinyl moiety by a PPTase is required for PCP activity (24,48,49). Another gene, phbB, located in the vicinity of phbH, likely encodes an aryl carrier protein that also requires a PPTase for its activity (23).…”
Section: Discussionmentioning
confidence: 99%
“…The disrupted phbH gene of NS414 encodes a PCP-containing thiolation domain. Covalent modification of PCPs with a 4Ј-phosphopantetheinyl moiety by a PPTase is required for PCP activity (24,48,49). Another gene, phbB, located in the vicinity of phbH, likely encodes an aryl carrier protein that also requires a PPTase for its activity (23).…”
Section: Discussionmentioning
confidence: 99%
“…A putative condensation domain between each pair of adenylation domains of two consecutive modules was thought to catalyze peptide bond formation (5). Optional domains can also carry out modifications of the activated amino acid, like epimerization (45,48) and N methylation (15,54). In addition to the domains mentioned above, a putative thioesterase domain, which might be involved in product release and/or cyclization of the peptide chain, was found in bacterial systems as an integrated part of the modules incorporating the C-terminal amino acid.…”
mentioning
confidence: 99%
“…Each module can be subdivided in domains. The activation domain (500 aa) belongs to the large family of adenylate-forming enzymes that includes firefly luciferase and acyl coenzyme A (acyl-CoA) synthetases and contains nine core sequences (named boxes A to I by Pfeifer et al [31]) identified as AMP, ATP-Mg binding, adenine binding, or ATPase sites (10,12,14,28,31,44,45,51). This domain is also involved in the specific recognition of a given hydroxy or amino acid (7).…”
mentioning
confidence: 99%
“…This domain is also involved in the specific recognition of a given hydroxy or amino acid (7). The activation domain is followed by the acyl carrier protein (ACP) domain (80 aa) containing the phosphopantetheinyl attachment site, LGGXSI (39,44,45,46). Recently a potential elongation domain (350 aa) containing the motif HHXXXDG, which is thought to be involved in acyl transfer, was identified (9).…”
mentioning
confidence: 99%
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