1oil
From Proteopedia
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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 [[1]], with EC number [3.1.1.3]. 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
Page seeded by OCA on Mon Oct 29 19:04:33 2007
