The crystal structure of triacylglycerol lipase from Pseudomonas glumae reveals a partially redundant catalytic aspartate.

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 Lett

journal_title

FEBS letters

authors

Noble ME,Cleasby A,Johnson LN,Egmond MR,Frenken LG

doi

10.1016/0014-5793(93)80310-q

subject

Has Abstract

pub_date

1993-09-27 00:00:00

pages

123-8

issue

1-2

eissn

0014-5793

issn

1873-3468

pii

0014-5793(93)80310-Q

journal_volume

331

pub_type

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