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1hqd

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Revision as of 09:40, 20 March 2008 by OCA (Talk | contribs)
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Image:1hqd.gif


PDB ID 1hqd

Drag the structure with the mouse to rotate
, resolution 2.30Å
Ligands: and
Activity: Triacylglycerol lipase, with EC number 3.1.1.3
Coordinates: save as pdb, mmCIF, xml



PSEUDOMONAS CEPACIA LIPASE COMPLEXED WITH TRANSITION STATE ANALOGUE OF 1-PHENOXY-2-ACETOXY BUTANE


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. 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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