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Alcohol dehydrogenase of class III: consistent patterns of structural and functional conservation in relation to class I and other proteins
Author(s) -
Hjelmqvist Lars,
Shafqat Jawed,
Siddiqi Abdur Rehman,
Jörnvall Hans
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)01043-e
Subject(s) - alcohol dehydrogenase , vertebrate , biology , biochemistry , dehydrogenase , class (philosophy) , myoglobin , lizard , enzyme , chemistry , zoology , gene , computer science , artificial intelligence
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.