Reptilian alcohol dehydrogenase Heterogeneity relevant to class multiplicity of the mammalian enzyme

FEBS Letters

Shafqat, Jawed²  Hjelmqvist, Lars²  Ericsson, Monica¹  Carlquist, Mats¹  Höög, Jan-Olov²  Siddiqi, Abdur Rehman²  Jörnvall, Hans² 

[1] Karo Bio AB, Box 4032, S-141 04 Huddinge, Sweden;Department of Chemistry I, Karolinska Institutet, S-104 01 Stockholm, Sweden

关键词: Enzyme family;    Alcohol dehydrogenase;    Isozymes;    Heterogeneity;    Amino acid exchanges;   

DOI  :  10.1016/0014-5793(92)80080-Z

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Liver alcohol dehydrogenase of the ethanol-active type (‘class I enzyme’) from the lizard, Uromastix hardwickii, was purified and screened for relationships with other vertebrate forms of the enzyme. Two differernt acetylated N-termini (acetyl-Gly and acetyl-Ser) and further positional differences already in the N-terminal segments establish the presence of two types of protein chain. The multiplicity is different from that hitherto detected within vertebrate class I alcohol dehydrogenase isozymes but typical of that which would be expected for subunits of different classes. In particular, relationships to class II or to class II-related forms appear likely. This may indicate yet further vertebrate alcohol dehydrogenase multiplicity or discovery of a class II non-mammalian enzyme. The results give prospects of defining gene duplications corresponding to more than one alcohol dehydrogenase class split to at an early vertebrate stage.

【 授权许可】

Unknown