| Title : The crystal structure of triacylglycerol lipase from Pseudomonas glumae reveals a partially redundant catalytic aspartate - Noble_1993_FEBS.Lett_331_123 |
| Author(s) : Noble ME , Cleasby A , Johnson LN , Egmond MR , Frenken LG |
| Ref : FEBS Letters , 331 :123 , 1993 |
|
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. |
| PubMedSearch : Noble_1993_FEBS.Lett_331_123 |
| PubMedID: 8405390 |
| Gene_locus related to this paper: burgl-lipas |
| Gene_locus | burgl-lipas |
| Structure | 1QGE 1TAH |
Noble ME, Cleasby A, Johnson LN, Egmond MR, Frenken LG (1993)
The crystal structure of triacylglycerol lipase from Pseudomonas glumae reveals a partially redundant catalytic aspartate
FEBS Letters
331 :123
Noble ME, Cleasby A, Johnson LN, Egmond MR, Frenken LG (1993)
FEBS Letters
331 :123