1het: Difference between revisions
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==About this Structure== | ==About this Structure== | ||
1HET is a | 1HET is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Equus_caballus Equus caballus] with ZN, NAD and MRD as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Alcohol_dehydrogenase Alcohol dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.1 1.1.1.1] Structure known Active Sites: AC3, AC4, NAA, NAB, OHA and OHB. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HET OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: oxidoreductase(nad(a)-choh(d))]] | [[Category: oxidoreductase(nad(a)-choh(d))]] | ||
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Revision as of 15:53, 5 November 2007
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ATOMIC X-RAY STRUCTURE OF LIVER ALCOHOL DEHYDROGENASE CONTAINING A HYDROXIDE ADDUCT TO NADH
OverviewOverview
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.
About this StructureAbout this Structure
1HET is a Single protein structure of sequence from Equus caballus with ZN, NAD and MRD as ligands. Active as Alcohol dehydrogenase, with EC number 1.1.1.1 Structure known Active Sites: AC3, AC4, NAA, NAB, OHA and OHB. 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
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