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1lbs

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{{STRUCTURE_1lbs| PDB=1lbs | SCENE= }}
{{STRUCTURE_1lbs| PDB=1lbs | SCENE= }}
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'''LIPASE (E.C.3.1.1.3) (TRIACYLGLYCEROL HYDROLASE)'''
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===LIPASE (E.C.3.1.1.3) (TRIACYLGLYCEROL HYDROLASE)===
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==Overview==
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Many lipases are potent catalysts of stereoselective reactions and are therefore of interest for use in chemical synthesis. The crystal structures of lipases show a large variation in the shapes of their active site environments that may explain the large variation in substrate specificity of these enzymes. We have determined the three-dimensional structure of Candida antarctica lipase B (CALB) cocrystallized with the detergent Tween 80. In another crystal form, the structure of the enzyme in complex with a covalently bound phosphonate inhibitor has been determined. In both structures, the active site is exposed to the external solvent. The potential lid-forming helix alpha 5 in CALB is well-ordered in the Tween 80 structure and disordered in the inhibitor complex. The tetrahedral intermediates of two chiral substrates have been modeled on the basis of available structural and biochemical information. The results of this study provide a structural explanation for the high stereoselectivity of CALB toward many secondary alcohols.
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{{ABSTRACT_PUBMED_8527460}}
==About this Structure==
==About this Structure==
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[[Category: Jones, T A.]]
[[Category: Jones, T A.]]
[[Category: Uppenberg, J.]]
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Revision as of 09:16, 2 July 2008

Image:1lbs.png

Template:STRUCTURE 1lbs

LIPASE (E.C.3.1.1.3) (TRIACYLGLYCEROL HYDROLASE)

Template:ABSTRACT PUBMED 8527460

About this Structure

1LBS is a Single protein structure of sequence from Candida antarctica. Full crystallographic information is available from OCA.

Reference

Crystallographic and molecular-modeling studies of lipase B from Candida antarctica reveal a stereospecificity pocket for secondary alcohols., Uppenberg J, Ohrner N, Norin M, Hult K, Kleywegt GJ, Patkar S, Waagen V, Anthonsen T, Jones TA, Biochemistry. 1995 Dec 26;34(51):16838-51. PMID:8527460

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