Studies on variants of alcohol dehydrogenases and its domains.

Abstract

Zinc-containing medium-chain alcohol dehydrogenases/reductases (MDR) are ubiquitous (Danielsson et al., 1994), constituting a group of enzymes with great multiplicity. Natural variants of the family serve to illustrate functional properties, but can also serve as tools for studying evolution of novel forms. Formation of families, enzymes, classes and isozymes reflects these aspects. Class III/glutathione-dependent formaldehyde dehydrogenase, with its constant properties in vertebrates (Jornvall and Hoog, 1995; Hjelmqvist et al., 1995), invertebrates (Danielsson et al., 1994; Kaiser et al., 1993), plants (Shafqat et al., 1996; Martinez et al., 1996), fungi (Sasnaukas et al., 1992; Fernandez et al., 1995), prokaryotes (Gutheil et al., 1992; Ras et al., 1995), and archaeons (Ammendola, 1992) has a distant origin. Class I, with ethanol dehydrogenase activity, has a duplicatory origin from class III (Daniels son and Jornvall, 1992; Jornvall, 1994), as has also the ethanol active ADH in plants (Shafqat et al., 1996). Different regions of the molecules have been assessed for various functional and structural properties, like binding of substrate and coenzyme (Eklund, 1984; Hurley, 1991), metals (Eklund et al., 1976), other subunits (Persson et al., 1993; Danielsson et al., 1994), and further aspects.