1LPP

ANALOGS OF REACTION INTERMEDIATES IDENTIFY A UNIQUE SUBSTRATE BINDING SITE IN CANDIDA RUGOSA LIPASE

1LPP の概要

• エントリーDOI: 10.2210/pdb1lpp/pdb
• 分子名称: LIPASE, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (6 entities in total)
• 機能のキーワード: hydrolase
• 由来する生物種: Candida rugosa (ascomycetes)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 59927.40

構造登録者

Grochulski, P.G.,Cygler, M.C. (登録日: 1995-01-17, 公開日: 1995-04-20, 最終更新日: 2024-10-23)

主引用文献

Grochulski, P.,Bouthillier, F.,Kazlauskas, R.J.,Serreqi, A.N.,Schrag, J.D.,Ziomek, E.,Cygler, M.
Analogs of reaction intermediates identify a unique substrate binding site in Candida rugosa lipase.
Biochemistry, 33:3494-3500, 1994

PubMed Abstract: The structures of Candida rugosa lipase-inhibitor complexes demonstrate that the scissile fatty acyl chain is bound in a narrow, hydrophobic tunnel which is unique among lipases studied to date. Modeling of triglyceride binding suggests that the bound lipid must adopt a "tuning fork" conformation. The complexes, analogs of tetrahedral intermediates of the acylation and deacylation steps of the reaction pathway, localize the components of the oxyanion hole and define the stereochemistry of ester hydrolysis. Comparison with other lipases suggests that the positioning of the scissile fatty acyl chain and ester bond and the stereochemistry of hydrolysis are the same in all lipases which share the alpha/beta-hydrolase fold.

PubMed: 8142346
DOI: 10.1021/bi00178a005

実験手法

X-RAY DIFFRACTION (2.18 Å)