1het: Difference between revisions

Revision as of 08:05, 1 July 2008

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File:1het.png

Template:STRUCTURE 1het

ATOMIC X-RAY STRUCTURE OF LIVER ALCOHOL DEHYDROGENASE CONTAINING A HYDROXIDE ADDUCT TO NADHATOMIC X-RAY STRUCTURE OF LIVER ALCOHOL DEHYDROGENASE CONTAINING A HYDROXIDE ADDUCT TO NADH

Template:ABSTRACT PUBMED 11134046

About this StructureAbout this Structure

1HET is a Single protein structure of sequence from Equus caballus. Full crystallographic information is available from OCA.

ReferenceReference

On the enzymatic activation of NADH., Meijers R, Morris RJ, Adolph HW, Merli A, Lamzin VS, Cedergren-Zeppezauer ES, J Biol Chem. 2001 Mar 23;276(12):9316-21. Epub 2000 Dec 28. PMID:11134046

Page seeded by OCA on Tue Jul 1 08:05:30 2008

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OCA

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-'''ATOMIC X-RAY STRUCTURE OF LIVER ALCOHOL DEHYDROGENASE CONTAINING A HYDROXIDE ADDUCT TO NADH'''
+===ATOMIC X-RAY STRUCTURE OF LIVER ALCOHOL DEHYDROGENASE CONTAINING A HYDROXIDE ADDUCT TO NADH===
-==Overview==
+<!--
-Atomic (1 A) resolution x-ray structures of horse liver alcohol dehydrogenase in complex with NADH revealed the formation of an adduct in the active site between a metal-bound water and NADH. Furthermore, a pronounced distortion of the pyridine ring of NADH was observed. A series of quantum chemical calculations on the water-nicotinamide adduct showed that the puckering of the pyridine ring in the crystal structures can only be reproduced when the water is considered a hydroxide ion. These observations provide fundamental insight into the enzymatic activation of NADH for hydride transfer.
+The line below this paragraph, {{ABSTRACT_PUBMED_11134046}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_11134046}}
 ==About this Structure==
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 [[Category: Merli, A.]]
 [[Category: Morris, R J.]]
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