3HUD

THE STRUCTURE OF HUMAN BETA 1 BETA 1 ALCOHOL DEHYDROGENASE: CATALYTIC EFFECTS OF NON-ACTIVE-SITE SUBSTITUTIONS

3HUD の概要

• エントリーDOI: 10.2210/pdb3hud/pdb
• 分子名称: ALCOHOL DEHYDROGENASE, ZINC ION, NICOTINAMIDE-ADENINE-DINUCLEOTIDE (3 entities in total)
• 機能のキーワード: oxidoreductase(nad(a)-choh(d))
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm: P00325
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 81135.04

構造登録者

Hurley, T.D.,Bosron, W.F.,Hamilton, J.A.,Amzel, L.M. (登録日: 1993-01-04, 公開日: 1994-01-31, 最終更新日: 2024-02-21)

主引用文献

Hurley, T.D.,Bosron, W.F.,Hamilton, J.A.,Amzel, L.M.
Structure of human beta 1 beta 1 alcohol dehydrogenase: catalytic effects of non-active-site substitutions.
Proc.Natl.Acad.Sci.USA, 88:8149-8153, 1991

PubMed Abstract: 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.

PubMed: 1896463
DOI: 10.1073/pnas.88.18.8149

実験手法

X-RAY DIFFRACTION (3.2 Å)