Download MendeleyThe crystal structure of a triacylglycerol lipase from Pseudomonas cepacia reveals a highly open conformation in the absence of a bound inhibitor.
Kim, K.K., Song, H.K., Shin, D.H., Hwang, K.Y., Suh, S.W.(1997) Structure 5: 173-185
- PubMed: 9032073
- DOI: https://doi.org/10.1016/s0969-2126(97)00177-9
- Primary Citation of Related Structures:
1OIL - PubMed Abstract:
. 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.
Organizational Affiliation:
Department of Chemistry, College of Natural Sciences, Seoul National University, Seoul 151-742, Korea.
