1e3v: Difference between revisions

Revision as of 00:06, 1 July 2008

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File:1e3v.png

Template:STRUCTURE 1e3v

CRYSTAL STRUCTURE OF KETOSTEROID ISOMERASE FROM PSEDOMONAS PUTIDA COMPLEXED WITH DEOXYCHOLATECRYSTAL STRUCTURE OF KETOSTEROID ISOMERASE FROM PSEDOMONAS PUTIDA COMPLEXED WITH DEOXYCHOLATE

Template:ABSTRACT PUBMED 11007792

About this StructureAbout this Structure

1E3V is a Single protein structure of sequence from Pseudomonas putida. Full crystallographic information is available from OCA.

ReferenceReference

Detection of large pKa perturbations of an inhibitor and a catalytic group at an enzyme active site, a mechanistic basis for catalytic power of many enzymes., Ha NC, Kim MS, Lee W, Choi KY, Oh BH, J Biol Chem. 2000 Dec 29;275(52):41100-6. PMID:11007792

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OCA

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 {{STRUCTURE_1e3v|  PDB=1e3v  |  SCENE=  }}
-'''CRYSTAL STRUCTURE OF KETOSTEROID ISOMERASE FROM PSEDOMONAS PUTIDA COMPLEXED WITH DEOXYCHOLATE'''
+===CRYSTAL STRUCTURE OF KETOSTEROID ISOMERASE FROM PSEDOMONAS PUTIDA COMPLEXED WITH DEOXYCHOLATE===
-==Overview==
+<!--
-Delta(5)-3-Ketosteroid isomerase catalyzes cleavage and formation of a C-H bond at a diffusion-controlled limit. By determining the crystal structures of the enzyme in complex with each of three different inhibitors and by nuclear magnetic resonance (NMR) spectroscopic investigation, we evidenced the ionization of a hydroxyl group (pK(a) approximately 16.5) of an inhibitor, which forms a low barrier hydrogen bond (LBHB) with a catalytic residue Tyr(14) (pK(a) approximately 11.5), and the protonation of the catalytic residue Asp(38) with pK(a) of approximately 4.5 at pH 6.7 in the interaction with a carboxylate group of an inhibitor. The perturbation of the pK(a) values in both cases arises from the formation of favorable interactions between inhibitors and catalytic residues. The results indicate that the pK(a) difference between catalytic residue and substrate can be significantly reduced in the active site environment as a result of the formation of energetically favorable interactions during the course of enzyme reactions. The reduction in the pK(a) difference should facilitate the abstraction of a proton and thereby eliminate a large fraction of activation energy in general acid/base enzyme reactions. The pK(a) perturbation provides a mechanistic ground for the fast reactivity of many enzymes and for the understanding of how some enzymes are able to extract a proton from a C-H group with a pK(a) value as high as approximately 30.
+The line below this paragraph, {{ABSTRACT_PUBMED_11007792}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 11007792 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_11007792}}
 ==About this Structure==
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 [[Category: Lbhb]]
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