Alcohol dehydrogenase of class III: consistent patterns of structural and functional conservation in relation to class I and other proteins

FEBS Letters

Shafqat, Jawed¹  Hjelmqvist, Lars¹  Siddiqi, Abdur Rehman¹  Jörnvall, Hans¹ 

[1]Department of Medical Biochemistry and Biophysics, Karolinska Institutet, S-171 77 Stockholm, Sweden

关键词: Alcohol dehydrogenase;    Reptilian protein;    Uromastix hardwickii;    Amino acid sequence;    Molecular evolution;   

DOI  :  10.1016/0014-5793(95)01043-E

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Class III alcohol dehydrogenase from the lizard Uromastix hardwickii has been characterized. This non-mammalian, gnathostomatous vertebrate class III form allows correlations of structures and functions of this class, the traditional class I alcohol dehydrogenase, and other well-studied proteins. Catalytically, results show similar recoveries and activities of all vertebrate class III forms independent of source, similar activities also in invertebrates but in lower amounts, and considerably higher specific activities in microorganisms. Structurally, variability patterns are consistent throughout the vertebrate system with a ratio in accepted point mutations versus class I of 0.4. This ratio between different classes of a zinc enzyme is comparable to that between different heme proteins (cytochrome c and myoglobin), suggesting defined but non-identical functions also for the alcohol dehydrogenase classes.

【 授权许可】

Unknown