1tah
From Proteopedia
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THE CRYSTAL STRUCTURE OF TRIACYLGLYCEROL LIPASE FROM PSEUDOMONAS GLUMAE REVEALS A PARTIALLY REDUNDANT CATALYTIC ASPARTATE
Overview
The family of lipases (triacylglycerol-acyl-hydrolases EC 3.1.1.3), constitutes an interesting class of enzymes because of their ability to, interact with lipid-water interfaces, their wide range of substrate, specificities, and their potential industrial applications. Here we report, the first crystal structure of a bacterial lipase, from Pseudomonas, glumae. The structure is formed from three domains, the largest of which, contains a subset of the alpha/beta hydrolase fold and a calcium site., Asp263, the acidic residue in the catalytic triad, has previously been, mutated into an alanine with only a modest reduction in activity.
About this Structure
1TAH is a Single protein structure of sequence from Burkholderia glumae with CA as ligand. Active as Triacylglycerol lipase, with EC number 3.1.1.3 Full crystallographic information is available from OCA.
Reference
The crystal structure of triacylglycerol lipase from Pseudomonas glumae reveals a partially redundant catalytic aspartate., Noble ME, Cleasby A, Johnson LN, Egmond MR, Frenken LG, FEBS Lett. 1993 Sep 27;331(1-2):123-8. PMID:8405390
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