L. Hjelmqvist et al., ALCOHOL-DEHYDROGENASE OF CLASS-III - CONSISTENT PATTERNS OF STRUCTURAL AND FUNCTIONAL CONSERVATION IN RELATION TO CLASS-I AND OTHER PROTEINS, FEBS letters, 373(3), 1995, pp. 212-216
Class III alcohol dehydrogenase from the lizard Uromastix hardwickii h
as 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 a
ctivities of all vertebrate class III forms independent of source, sim
ilar activities also in invertebrates but in lower amounts, and consid
erably higher specific activities in microorganisms, Structurally, var
iability 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 betw
een different heme proteins (cytochrome c and myoglobin), suggesting d
efined but non-identical functions also for the alcohol dehydrogenase
classes.