1lpn

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{{STRUCTURE_1lpn| PDB=1lpn | SCENE= }}
{{STRUCTURE_1lpn| PDB=1lpn | SCENE= }}
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'''ANALOGS OF REACTION INTERMEDIATES IDENTIFY A UNIQUE SUBSTRATE BINDING SITE IN CANDIDA RUGOSA LIPASE'''
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===ANALOGS OF REACTION INTERMEDIATES IDENTIFY A UNIQUE SUBSTRATE BINDING SITE IN CANDIDA RUGOSA LIPASE===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 8142346 is the PubMed ID number.
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{{ABSTRACT_PUBMED_8142346}}
==About this Structure==
==About this Structure==
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[[Category: Grochulski, P G.]]
[[Category: Grochulski, P G.]]
[[Category: Hydrolase]]
[[Category: Hydrolase]]
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Revision as of 18:44, 2 July 2008

Image:1lpn.png

Template:STRUCTURE 1lpn

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

Template:ABSTRACT PUBMED 8142346

About this Structure

1LPN is a Single protein structure. 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

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