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'''THE CRYSTAL STRUCTURE OF TRIACYLGLYCEROL LIPASE FROM PSEUDOMONAS GLUMAE REVEALS A PARTIALLY REDUNDANT CATALYTIC ASPARTATE''' | '''THE CRYSTAL STRUCTURE OF TRIACYLGLYCEROL LIPASE FROM PSEUDOMONAS GLUMAE REVEALS A PARTIALLY REDUNDANT CATALYTIC ASPARTATE''' | ||
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[[Category: Johnson, L N.]] | [[Category: Johnson, L N.]] | ||
[[Category: Noble, M E.M.]] | [[Category: Noble, M E.M.]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 09:44:29 2008'' | |||
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Revision as of 06:44, 3 May 2008
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. 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 Page seeded by OCA on Sat May 3 09:44:29 2008
