1lbs
From Proteopedia
(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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| - | [[Image:1lbs.jpg|left|200px]]<br /><applet load="1lbs" size=" | + | [[Image:1lbs.jpg|left|200px]]<br /><applet load="1lbs" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1lbs, resolution 2.6Å" /> | caption="1lbs, resolution 2.6Å" /> | ||
'''LIPASE (E.C.3.1.1.3) (TRIACYLGLYCEROL HYDROLASE)'''<br /> | '''LIPASE (E.C.3.1.1.3) (TRIACYLGLYCEROL HYDROLASE)'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Many lipases are potent catalysts of stereoselective reactions and are | + | 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== | ==About this Structure== | ||
| - | 1LBS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Candida_antarctica Candida antarctica] with HEE as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http:// | + | 1LBS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Candida_antarctica Candida antarctica] with <scene name='pdbligand=HEE:'>HEE</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LBS OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Triacylglycerol lipase]] | [[Category: Triacylglycerol lipase]] | ||
| - | [[Category: Jones, T | + | [[Category: Jones, T A.]] |
[[Category: Uppenberg, J.]] | [[Category: Uppenberg, J.]] | ||
[[Category: HEE]] | [[Category: HEE]] | ||
[[Category: hydrolase (carboxylic esterase)]] | [[Category: hydrolase (carboxylic esterase)]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:43:28 2008'' |
Revision as of 11:43, 21 February 2008
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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 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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