Abstract:
: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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Noble ME,Cleasby A,Johnson LN,Egmond MR,Frenken LGdoi
10.1016/0014-5793(93)80310-qsubject
Has Abstractpub_date
1993-09-27 00:00:00pages
123-8issue
1-2eissn
0014-5793issn
1873-3468pii
0014-5793(93)80310-Qjournal_volume
331pub_type
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