1lbs

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[[Image:1lbs.jpg|left|200px]]
[[Image:1lbs.jpg|left|200px]]
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{{Structure
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<!--
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|PDB= 1lbs |SIZE=350|CAPTION= <scene name='initialview01'>1lbs</scene>, resolution 2.6&Aring;
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The line below this paragraph, containing "STRUCTURE_1lbs", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=HEE:N-HEXYLPHOSPHONATE+ETHYL+ESTER'>HEE</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Triacylglycerol_lipase Triacylglycerol lipase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.3 3.1.1.3] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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-->
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|DOMAIN=
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{{STRUCTURE_1lbs| PDB=1lbs | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1lbs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lbs OCA], [http://www.ebi.ac.uk/pdbsum/1lbs PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1lbs RCSB]</span>
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}}
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'''LIPASE (E.C.3.1.1.3) (TRIACYLGLYCEROL HYDROLASE)'''
'''LIPASE (E.C.3.1.1.3) (TRIACYLGLYCEROL HYDROLASE)'''
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[[Category: Jones, T A.]]
[[Category: Jones, T A.]]
[[Category: Uppenberg, J.]]
[[Category: Uppenberg, J.]]
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[[Category: hydrolase (carboxylic esterase)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 23:45:53 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:00:49 2008''
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Revision as of 20:45, 2 May 2008

Image:1lbs.jpg

Template:STRUCTURE 1lbs

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. 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 Page seeded by OCA on Fri May 2 23:45:53 2008

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