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The crystal structure of triacylglycerol lipase from Pseudomonas glumae reveals a partially redundant catalytic aspartate
Author(s) -
Noble M.E.M.,
Cleasby A.,
Johnson L.N.,
Egmond M.R.,
Frenken L.G.J.
Publication year - 1993
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(93)80310-q
Subject(s) - lipase , catalytic triad , hydrolase , pseudomonas , residue (chemistry) , enzyme , chemistry , crystal structure , biochemistry , alanine , catalysis , stereochemistry , active site , substrate (aquarium) , crystallography , biology , amino acid , bacteria , genetics , ecology
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 [1,2]. 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 α/β hydrolase fold and a calcium site. Asp 263 , the acidic residue in the catalytic triad, has previously been mutated into an alanine with only a modest reduction in activity [3].