Title : The crystal structure of a triacylglycerol lipase from Pseudomonas cepacia reveals a highly open conformation in the absence of a bound inhibitor - Kim_1997_Structure_5_173 |
Author(s) : Kim KK , Song HK , Shin DH , Hwang KY , Suh SW |
Ref : Structure , 5 :173 , 1997 |
Abstract :
BACKGROUND:
Lipases, a family of enzymes which catalyze the hydrolysis of triglycerides, are widely distributed in many organisms. True lipases are distinguished from esterases by the characteristic interfacial activation they exhibit at an oil-water interface. Lipases are one of the most frequently used biocatalysts for organic reactions performed under mild conditions. Their biotechnological applications include food and oil processing and the preparation of chiral intermediates for the synthesis of enantiomerically pure pharmaceuticals. Recent structural studies on several lipases have provided some clues towards understanding the mechanisms of hydrolytic activity, interfacial activation, and stereoselectivity. This study was undertaken in order to provide structural information on bacterial lipases, which is relatively limited in comparison to that on the enzymes from other sources.
RESULTS:
We have determined the crystal structure of a triacylglycerol lipase from Pseudomonas cepacia (PcL) in the absence of a bound inhibitor using X-ray crystallography. The structure shows the lipase to contain an alpha/beta-hydrolase fold and a catalytic triad comprising of residues Ser87, His286 and Asp264. The enzyme shares several structural features with homologous lipases from Pseudomonas glumae (PgL) and Chromobacterium viscosum (CvL), including a calcium-binding site. The present structure of PcL reveals a highly open conformation with a solvent-accessible active site. This is in contrast to the structures of PgL and PcL in which the active site is buried under a closed or partially opened 'lid', respectively.
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PubMedSearch : Kim_1997_Structure_5_173 |
PubMedID: 9032073 |
Gene_locus related to this paper: burce-lipaa |
Gene_locus | burce-lipaa |
Structure | burce-lipaa 1OIL |
Kim KK, Song HK, Shin DH, Hwang KY, Suh SW (1997)
The crystal structure of a triacylglycerol lipase from Pseudomonas cepacia reveals a highly open conformation in the absence of a bound inhibitor
Structure
5 :173
Kim KK, Song HK, Shin DH, Hwang KY, Suh SW (1997)
Structure
5 :173