1lpn
From Proteopedia
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ANALOGS OF REACTION INTERMEDIATES IDENTIFY A UNIQUE SUBSTRATE BINDING SITE IN CANDIDA RUGOSA LIPASE
Overview
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.
About this Structure
1LPN is a Single protein structure of sequence from [1] with , and as ligands. Active as Triacylglycerol lipase, with EC number 3.1.1.3 Full crystallographic information is available from OCA.
Reference
Analogs of reaction intermediates identify a unique substrate binding site in Candida rugosa lipase., Grochulski P, Bouthillier F, Kazlauskas RJ, Serreqi AN, Schrag JD, Ziomek E, Cygler M, Biochemistry. 1994 Mar 29;33(12):3494-500. PMID:8142346
Page seeded by OCA on Thu Feb 21 13:47:16 2008
Categories: Single protein | Triacylglycerol lipase | Cygler, M C. | Grochulski, P G. | CA | DSC | NAG | Hydrolase
