Structural highlights
Function
LIP_BURCE Catalyzes the hydrolysis of triglycerides.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
In a series of four racemic phenoxyalkyl-alkyl carbinols, 1-phenoxy-2-hydroxybutane (1) is enantioselectively acetylated by Burkholderia cepacia (formerly Pseudomonas cepacia) lipase with an E value > or = 200, whereas for the other three racemates E was found to be < or = 4. To explain the high preference of B. cepacia lipase for (R)-(+)-1, a precursor of its transition state analogue with a tetrahedral P-atom, (R(P),S(P))-O-(2R)-(1-phenoxybut-2-yl)methylphosphonic acid chloride was prepared and crystallized in complex with B. cepacia lipase. The X-ray structure of the complex was determined, allowing to compare the conformation of the inhibitor with results of molecular modelling.
Complex of Burkholderia cepacia lipase with transition state analogue of 1-phenoxy-2-acetoxybutane: biocatalytic, structural and modelling study.,Luic M, Tomic S, Lescic I, Ljubovic E, Sepac D, Sunjic V, Vitale L, Saenger W, Kojic-Prodic B Eur J Biochem. 2001 Jul;268(14):3964-73. PMID:11453990[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Luic M, Tomic S, Lescic I, Ljubovic E, Sepac D, Sunjic V, Vitale L, Saenger W, Kojic-Prodic B. Complex of Burkholderia cepacia lipase with transition state analogue of 1-phenoxy-2-acetoxybutane: biocatalytic, structural and modelling study. Eur J Biochem. 2001 Jul;268(14):3964-73. PMID:11453990
