The crystal structure of triacylglycerol lipase from Pseudomonas glumae reveals a partially redundant catalytic aspartate.
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.
Noble
M E
ME
Laboratory of Molecular Biophysics, Department of Biochemistry, Oxford, UK.
Cleasby
A
A
Johnson
L N
LN
Egmond
M R
MR
Frenken
L G
LG
D000595:Amino Acid Sequence; D001224:Aspartic Acid / Q000032:analysis*; D002384:Catalysis; D003460:Crystallization; D008049:Lipase / Q000737:chemistry*; D008969:Molecular Sequence Data; D011487:Protein Conformation; D011549:Pseudomonas / Q000201:enzymology*
D001224:Aspartic Acid; D008049:Lipase