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1GJP

SCHIFF-BASE COMPLEX OF YEAST 5-AMINOLAEVULINIC ACID DEHYDRATASE WITH 4-OXOSEBACIC ACID

1GJP の概要
エントリーDOI10.2210/pdb1gjp/pdb
関連するPDBエントリー1AW5 1EB3 1H7N 1H7O 1H7P 1H7R 1QML 1QNV 1YLV
分子名称5-AMINOLAEVULINIC ACID DEHYDRATASE, 4-OXODECANEDIOIC ACID, ZINC ION, ... (4 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37823.58
構造登録者
Erskine, P.T.,Coates, L.,Newbold, R.,Brindley, A.A.,Wood, S.P.,Warren, M.J.,Cooper, J.B.,Shoolingin-Jordan, P.M.,Neier, R. (登録日: 2001-08-01, 公開日: 2001-08-02, 最終更新日: 2024-11-13)
主引用文献Erskine, P.T.,Coates, L.,Newbold, R.,Brindley, A.A.,Stauffer, F.,Wood, S.P.,Warren, M.J.,Cooper, J.B.,Shoolingin-Jordan, P.M.,Neier, R.
The X-Ray Structure of Yeast 5-Aminolaevulinic Acid Dehydratase Complexed with Two Diacid Inhibitors
FEBS Lett., 503:196-, 2001
Cited by
PubMed Abstract: The structures of 5-aminolaevulinic acid dehydratase complexed with two irreversible inhibitors (4-oxosebacic acid and 4,7-dioxosebacic acid) have been solved at high resolution. Both inhibitors bind by forming a Schiff base link with Lys 263 at the active site. Previous inhibitor binding studies have defined the interactions made by only one of the two substrate moieties (P-side substrate) which bind to the enzyme during catalysis. The structures reported here provide an improved definition of the interactions made by both of the substrate molecules (A- and P-side substrates). The most intriguing result is the novel finding that 4,7-dioxosebacic acid forms a second Schiff base with the enzyme involving Lys 210. It has been known for many years that P-side substrate forms a Schiff base (with Lys 263) but until now there has been no evidence that binding of A-side substrate involves formation of a Schiff base with the enzyme. A catalytic mechanism involving substrate linked to the enzyme through Schiff bases at both the A- and P-sites is proposed.
PubMed: 11513881
DOI: 10.1016/S0014-5793(01)02721-1
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.8 Å)
構造検証レポート
Validation report summary of 1gjp
検証レポート(詳細版)ダウンロードをダウンロード

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件を2024-12-18に公開中

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