Dual relationships of xylitol and alcohol dehydrogenases in families of two protein types

• Published in: FEBS letters 1993-06, Vol.324 (1), p.9-14
• Main Authors: Persson, Bengt, Hallborn, Johan, Walfridsson, Mats, Hahn-Hägerdal, Bärbel, Keränen, Sirkka, Penttilä, Merja, Jörnvall, Hans
• Format: Article
• Language: English
• Subjects: Active site; Alcohol Dehydrogenase - genetics; Alcohol Dehydrogenase - metabolism; Alcohol Oxidoreductases - genetics; Amino Acid Sequence; Animals; Binding Sites; Biological and medical sciences; D-Xylulose Reductase; Enzyme relationship; Fundamental and applied biological sciences. Psychology; Genes, Fungal; Genes. Genome; Humans; L-Iditol 2-Dehydrogenase - genetics; Ligands; Molecular and cellular biology; Molecular genetics; Molecular Sequence Data; Multigene Family; Mutagenesis, Insertional; Pichia - enzymology; Pichia - genetics; Protein family: Homology; Sequence Deletion; Sequence Homology, Amino Acid; Short-chain dehydrogenase: Medium-chain alcohol dehydrogenase; Sugar Alcohol Dehydrogenases - genetics; Sugar Alcohol Dehydrogenases - metabolism; Zinc - metabolism
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/0014-5793(93)81522-2

Xylitol dehydrogenase encoded by gene XYL2 from Pichia stipitis is a member of the medium-chain alcohol dehydrogenase family, as evidenced by the domain organization and a distant homology (24% residue identity with the human class I γ 1 alcohol dehydrogenase). Much of a loop structure is missing, like in mammalian sorbitol and prokaryotic threonine dehydrogenases, many additional differences occur, and relationships are closest with the sorbitol dehydrogenase, the equivalence of which in P. stipitis may actually be the xylitol dehydrogenase. A second P. stipitis gene, also cloned and corresponding to a xylitol dehydrogenase, is highly different from XYL2, but encodes an enzyme with structural properties typical of the short-chain dehydrogenase family, which also contains an alcohol dehydrogenase (from Drosophila). Thus, yeast xylitol dehydrogenases, like alcohol and polyol dehydrogenases from other sources, have dual derivations, combining similar enzyme activities in separate protein families. In contrast to the situation with the other enzymes, both forms of xylitol dehydrogenase are present in one organism.