1ohl: Difference between revisions

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==Overview==
==Overview==
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.
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 Structure==
==About this Structure==
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[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Brindley, A.A.]]
[[Category: Brindley, A A.]]
[[Category: Butler, D.]]
[[Category: Butler, D.]]
[[Category: Coates, L.]]
[[Category: Coates, L.]]
[[Category: Cooper, J.B.]]
[[Category: Cooper, J B.]]
[[Category: Erskine, P.T.]]
[[Category: Erskine, P T.]]
[[Category: Shoolingin-Jordan, P.M.]]
[[Category: Shoolingin-Jordan, P M.]]
[[Category: Warren, M.J.]]
[[Category: Warren, M J.]]
[[Category: Wood, S.P.]]
[[Category: Wood, S P.]]
[[Category: Youell, J.H.]]
[[Category: Youell, J H.]]
[[Category: BME]]
[[Category: BME]]
[[Category: PBG]]
[[Category: PBG]]
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[[Category: tim barrel]]
[[Category: tim barrel]]


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Revision as of 15:17, 21 February 2008

File:1ohl.jpg


1ohl, resolution 1.6Å

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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 , and as ligands. Active as Porphobilinogen synthase, with EC number 4.2.1.24 Known structural/functional Site: . 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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