1mj3: Difference between revisions

Revision as of 00:05, 3 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1mj3.png

Template:STRUCTURE 1mj3

Crystal Structure Analysis of rat enoyl-CoA hydratase in complex with hexadienoyl-CoACrystal Structure Analysis of rat enoyl-CoA hydratase in complex with hexadienoyl-CoA

Template:ABSTRACT PUBMED 12445775

About this StructureAbout this Structure

1MJ3 is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.

ReferenceReference

Stereoselectivity of enoyl-CoA hydratase results from preferential activation of one of two bound substrate conformers., Bell AF, Feng Y, Hofstein HA, Parikh S, Wu J, Rudolph MJ, Kisker C, Whitty A, Tonge PJ, Chem Biol. 2002 Nov;9(11):1247-55. PMID:12445775

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-'''Crystal Structure Analysis of rat enoyl-CoA hydratase in complex with hexadienoyl-CoA'''
+===Crystal Structure Analysis of rat enoyl-CoA hydratase in complex with hexadienoyl-CoA===
-==Overview==
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-Enoyl-CoA hydratase catalyzes the hydration of trans-2-crotonyl-CoA to 3(S)- and 3(R)-hydroxybutyryl-CoA with a stereoselectivity (3(S)/3(R)) of 400,000 to 1. Importantly, Raman spectroscopy reveals that both the s-cis and s-trans conformers of the substrate analog hexadienoyl-CoA are bound to the enzyme, but that only the s-cis conformer is polarized. This selective polarization is an example of ground state strain, indicating the existence of catalytically relevant ground state destabilization arising from the selective complementarity of the enzyme toward the transition state rather than the ground state. Consequently, the stereoselectivity of the enzyme-catalyzed reaction results from the selective activation of one of two bound substrate conformers rather than from selective binding of a single conformer. These findings have important implications for inhibitor design and the role of ground state interactions in enzyme catalysis.
+The line below this paragraph, {{ABSTRACT_PUBMED_12445775}}, adds the Publication Abstract to the page
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 [[Category: Wu, J.]]
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