Class IV alcohol dehydrogenase (the gastric enzyme) Structural analysis of human σσ‐ADH reveals class IV to be variable and confirms the presence of a fifth mammalian alcohol dehydrogenase class

FEBS Letters

Saubi, Narcis¹  Moreno, Alberto¹  Parés, Xavier¹  Cederlund, Ella²  Hóóg, Jan-Olov²  Jörnvall, Hans² 

[1] Departament de Bioquímica i Biologia Molecular, Facultat de Cieíncies, Universitat Autònoma de Barcelona, 08193 Bellaterra Barcelona, Spain;Department of Chemistry I, Karolinska Institutet, S-104 01 Stockholm, Sweden

关键词: Gastric alcohol dehydrogenase;    Alcohol dehydrogenase classes;    Enzyme evolution;    Gene duplication;    Conserved and variable enzymes;   

DOI  :  10.1016/0014-5793(92)80479-Z

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Human gastric alcohol dehydrogenase (σσ-ADH) was submitted to peptide analysis at picomole scale. A total of 72 positions were determined in the protein chain, providing information on three aspects of alcohol dehydrogenase structures in general. First, the data establish the presence of a unique class of the enzyme, now confirmed as class IV, expressed in gastric tissue and separate from another novel class. now termed class V. Second, the class IV gastric enzyme has active site relationships compatible with an ethanol-active, zinc-containing alcohol dehydrogenase. Third, this enzyme class is of the variable type, like that for the ‘variable’, classical liver alcohol dehydrogenase of class I, and in contrast to that for the ‘constant’ class III enzyme. Known human alcohol dehydrogenase structures now prove the presence of at least seven human genes for the enzyme and nine for the whole protein family.

【 授权许可】

Unknown