1lbs
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(New page: 200px<br /><applet load="1lbs" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lbs, resolution 2.6Å" /> '''LIPASE (E.C.3.1.1.3) ...)
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Revision as of 18:20, 20 November 2007
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LIPASE (E.C.3.1.1.3) (TRIACYLGLYCEROL HYDROLASE)
Overview
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.
About this Structure
1LBS is a Single protein structure of sequence from Candida antarctica with HEE as ligand. Active as Triacylglycerol lipase, with EC number 3.1.1.3 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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