1hqd | pdb_00001hqd
PSEUDOMONAS CEPACIA LIPASE COMPLEXED WITH TRANSITION STATE ANALOGUE OF 1-PHENOXY-2-ACETOXY BUTANE
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Overview
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.
About this Structure
1HQD is a Single protein structure of sequence from Burkholderia cepacia with CA and INK as ligands. Active as Triacylglycerol lipase, with EC number 3.1.1.3 Full crystallographic information is available from OCA.
Reference
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
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