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Revision as of 17:49, 5 November 2007
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YEAST 5-AMINOLAEVULINIC ACID DEHYDRATASE PUTATIVE CYCLIC REACTION INTERMEDIATE COMPLEX
OverviewOverview
The X-ray structure of yeast 5-aminolaevulinic acid dehydratase, in which, the catalytic site of the enzyme is complexed with a putative cyclic, intermediate composed of both substrate moieties, has been solved at 0.16, nm (1.6 A) resolution. The cyclic intermediate is bound covalently to, Lys(263) with the amino group of the aminomethyl side chain ligated to the, active-site zinc ion in a position normally occupied by a catalytic, hydroxide ion. The cyclic intermediate is catalytically competent, as, shown by its turnover in the presence of added substrate to form, porphobilinogen. The findings, combined with those of previous studies, are consistent with a catalytic mechanism in which the C-C bond linking, both substrates in the intermediate is formed before the C-N bond.
About this StructureAbout this Structure
1OHL is a Single protein structure of sequence from Saccharomyces cerevisiae with ZN, BME and PBG as ligands. Active as Porphobilinogen synthase, with EC number 4.2.1.24 Structure known Active Site: AC1. Full crystallographic information is available from OCA.
ReferenceReference
X-ray structure of a putative reaction intermediate of 5-aminolaevulinic acid dehydratase., Erskine PT, Coates L, Butler D, Youell JH, Brindley AA, Wood SP, Warren MJ, Shoolingin-Jordan PM, Cooper JB, Biochem J. 2003 Aug 1;373(Pt 3):733-8. PMID:12777167
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