Avian alcohol dehydrogenase. Characterization of the quail enzyme, functional interpretations, and relationships to the different classes of mammalian alcohol dehydrogenase

Abstract

The primary structure of the major quail liver alcohol dehydrogenase was determined. It is a long-chain, zinc-containing alcohol dehydrogenase of the type occurring also in mammals and hence allows judgement of the gene duplications giving rise to the classes of the human alcohol dehydrogenase system. The avian form is most closely related to the class I mammalian enzyme (72-75% residue identity), least related to class II (60% identity), and intermediately related to class III (64-65% identity). This pattern distinguishes the mammalian enzyme classes and separates classes I and II in particular. In addition to the generally larger similarities with class I, the avian enzyme exhibits certain residue patterns otherwise typical of the other classes, including an extra Trp residue, present in both class II and III but not in class I, with a corresponding increase in the UV absorbance. The avian enzyme further shows that a Gly residue at position 260 previously considered strictly conserved in alcohol dehydrogenases can be exchanged with Lys. However, zinc-binding residues, coenzyme-binding residues, and to a large extent substrate-binding residues are unchanged in the avian enzyme, suggesting its functional properties to be related to those of the class I mammalian alcohol dehydrogenases. In contrast, the areas of subunit interactions in the dimers differ substantially. These results show that (a) the vertebrate enzyme classes are of distant origin, (b) the submammalian enzyme exhibits partly mixed properties in relation to the classes, and (c) the three mammalian enzyme classes are not as equidistantly related as initially apparent but suggest origins from two sublevels.

Novel vascular cell-specific genes whose expression is regulated temporally and spatially during vascular system development.

“…Figure 6 shows the vascular structure in a Zinnia seedling based on a number of sections stained with phloroglucinol or toluidine blue, including those used for in situ hybridization experiments. Cells were uniform in the section taken from near TED2 ze ta-crysta I li n ADH human class I 1 ADH quail ADH frog ADH human class 111 ADH horse class 111 ADH rat class 111 ADH white clover ADH pea ADH strawberry A part of the predicted TED2 polypeptide residues 58 to 86 is aligned with C,-crystallin protein and several enzymes of the ADH family, including human class II ADH (Hoog et al, 1987), quail ADH (Kaiser et al, 1990), frog ADH (Cederlund et al, 1991), human class 111 ADH (Kaiser et al, 1988;Sharma et al, 1989), horse class 111 ADH (Kaiser et al, 1989), rat class 111 ADH (Julia et al, 1988), white clover ADHl (Ellison et al, 1990), pea ADHl (Llewellyn et al, 1987), and strawberry ADH (Wolyn and Jelenkovic, 1990). Amino acid sequences are shown using the single-letter code.…”

Diversity of Vertebrate Class I Alcohol Dehydrogenase

“…The other concerns relationships of all 18 class I alcohol dehydrogenases now characterized from two vertebrate classes, mammals and birds, 14 mammalian enzymes [lo, 181, including the allelic variants (PJ p2/ p3 and y1/y2) of the human isozymes, and 4 avian enzymes (Fig. 2, and [21,22,241). Both these properties bear on functional aspects of alcohol dehydrogenases, as discussed below, and are of additional interest in relation to properties of other proteins…”

“…In spite of these facts, species correlations also show that further positions are important for overall enzymic properties. Thus, the quail enzyme [22] has a branched-chain residue at position 141 (Ile) and Arg at position 271, like the chicken enzyme, but a high K, for ethanol (8.1 mM [29]), Parallel evolutionary changes in different enzyme lines, constant functional properties also of the structurally variable class I alcohol dehydrogenase Arrangement of each of the groups of the mammalian and avian alcohol dehydrogenase class I enzymes into phylogenetic trees gives the patterns shown in Fig. 3.…”

Estrogen induction of alcohol dehydrogenase in the uropygial gland of mallard ducks

“…A comparison of the human and horse ADH p subunit has been reported to show substitutions in 48 of the total 374 amino acid residues with the degree of identity being 87.4% [27]. Recently Kaiser et al [37] have characterized the quail liver enzyme and found it to be related most closely to the human class I enzyme (72-75% identity to they subunit) with some features of the class 111 enzyme. A comparison of the deduced amino acid sequence of DGHl with the protein sequence of the avian enzyme showed 88% identity.…”