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3hud
From Proteopedia
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THE STRUCTURE OF HUMAN BETA 1 BETA 1 ALCOHOL DEHYDROGENASE: CATALYTIC EFFECTS OF NON-ACTIVE-SITE SUBSTITUTIONS
Contents |
Overview
The three-dimensional structure of human beta 1 beta 1 alcohol, dehydrogenase (ADH; EC 1.1.1.1) complexed with NAD+ has been determined by, x-ray crystallography to 3.0-A resolution. The amino acids directly, involved in coenzyme binding are conserved between horse EE and human beta, 1 beta 1 alcohol dehydrogenase in all but one case [serine (horse) vs., threonine (human) at position 48]. As a result, the coenzyme molecule is, bound in a similar manner in the two enzymes. However, the strength of the, interactions in the vicinity of the pyrophosphate bridge of NAD+ appears, to be enhanced in the human enzyme. Side-chain movements of Arg-47 and, Asp-50 and a shift in the position of the helix comprising residues, 202-212 may explain both the decreased Vmax and the decreased rate of NADH, dissociation observed in the human enzyme vs. the horse enzyme. It appears, that these catalytic differences are not due to substitutions of any amino, acids directly involved in coenzyme binding but are the result of, structural rearrangements resulting from multiple sequence differences, between the two enzymes.
Disease
Known diseases associated with this structure: Alcoholism, susceptibility to OMIM:[103720]
About this Structure
3HUD is a Single protein structure of sequence from Homo sapiens with ZN and NAD as ligands. Active as Alcohol dehydrogenase, with EC number 1.1.1.1 Full crystallographic information is available from OCA.
Reference
Structure of human beta 1 beta 1 alcohol dehydrogenase: catalytic effects of non-active-site substitutions., Hurley TD, Bosron WF, Hamilton JA, Amzel LM, Proc Natl Acad Sci U S A. 1991 Sep 15;88(18):8149-53. PMID:1896463
Page seeded by OCA on Mon Nov 12 23:48:57 2007
