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1OHL

YEAST 5-AMINOLAEVULINIC ACID DEHYDRATASE PUTATIVE CYCLIC REACTION INTERMEDIATE COMPLEX

1OHL の概要
エントリーDOI10.2210/pdb1ohl/pdb
関連するPDBエントリー1AW5 1EB3 1GJP 1H7N 1H7O 1H7P 1H7R 1QML 1QNV 1YLV
分子名称DELTA-AMINOLEVULINIC ACID DEHYDRATASE, ZINC ION, BETA-MERCAPTOETHANOL, ... (5 entities in total)
機能のキーワードlyase, dehydratase, aldolase, tim barrel, tetrapyrrole synthesis
由来する生物種SACCHAROMYCES CEREVISIAE (BAKER'S YEAST)
タンパク質・核酸の鎖数1
化学式量合計38154.93
構造登録者
Erskine, P.T.,Coates, L.,Butler, D.,Youell, J.H.,Brindley, A.A.,Wood, S.P.,Warren, M.J.,Shoolingin-Jordan, P.M.,Cooper, J.B. (登録日: 2003-05-27, 公開日: 2003-06-02, 最終更新日: 2025-10-01)
主引用文献Erskine, P.T.,Coates, L.,Butler, D.,Youell, J.H.,Brindley, A.A.,Wood, S.P.,Warren, M.J.,Shoolingin-Jordan, P.M.,Cooper, J.B.
X-Ray Structure of a Putative Reaction Intermediateof 5-Aminolaevulinic Acid Dehydratase
Biochem.J., 373:733-, 2003
Cited by
PubMed Abstract: 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.
PubMed: 12777167
DOI: 10.1042/BJ20030513
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.6 Å)
構造検証レポート
Validation report summary of 1ohl
検証レポート(詳細版)ダウンロードをダウンロード

250059

件を2026-03-04に公開中

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