1oil
From Proteopedia
(New page: 200px<br /> <applet load="1oil" size="450" color="white" frame="true" align="right" spinBox="true" caption="1oil, resolution 2.10Å" /> '''STRUCTURE OF LIPASE...) |
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==About this Structure== | ==About this Structure== | ||
| - | 1OIL is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Burkholderia_cepacia Burkholderia cepacia]] with CA as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/ ]], 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OIL OCA]]. | + | 1OIL is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Burkholderia_cepacia Burkholderia cepacia]] with CA 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]]. Structure known Active Sites: ACT and BCT. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OIL OCA]]. |
==Reference== | ==Reference== | ||
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[[Category: Burkholderia cepacia]] | [[Category: Burkholderia cepacia]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| + | [[Category: Triacylglycerol lipase]] | ||
[[Category: Kim, K.K.]] | [[Category: Kim, K.K.]] | ||
[[Category: Shin, D.H.]] | [[Category: Shin, D.H.]] | ||
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[[Category: triacylglycerol lipase]] | [[Category: triacylglycerol lipase]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 12:18:35 2007'' |
Revision as of 10:13, 30 October 2007
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STRUCTURE OF LIPASE
Overview
BACKGROUND:. Lipases, a family of enzymes which catalyze the hydrolysis of, triglycerides, are widely distributed in many organisms. True lipases are, distinguished from esterases by the characteristic interfacial activation, they exhibit at an oil-water interface. Lipases are one of the most, frequently used biocatalysts for organic reactions performed under mild, conditions. Their biotechnological applications include food and oil, processing and the preparation of chiral intermediates for the synthesis, of enantiomerically pure pharmaceuticals. Recent structural studies on, several lipases have provided some clues towards understanding the, mechanisms of hydrolytic activity, interfacial activation, and, stereoselectivity. This study was undertaken in order to provide, structural ... [(full description)]
About this Structure
1OIL is a [Single protein] structure of sequence from [Burkholderia cepacia] with CA as [ligand]. Active as [Triacylglycerol lipase], with EC number [3.1.1.3]. Structure known Active Sites: ACT and BCT. Full crystallographic information is available from [OCA].
Reference
The crystal structure of a triacylglycerol lipase from Pseudomonas cepacia reveals a highly open conformation in the absence of a bound inhibitor., Kim KK, Song HK, Shin DH, Hwang KY, Suh SW, Structure. 1997 Feb 15;5(2):173-85. PMID:9032073
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