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



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



Febs (federation Of European Biochemical Societies) Letters. 324(1): 9-14



Xylitol dehydrogenase encoded by gene XYL2 from Pichia stipitis is a member of the medium-chain alcohol dehydrogenase family, as evidence by the domain organization and a distant homology (24% residue identity with the human class I-gamma-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.

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Accession: 008505760

Download citation: RISBibTeXText

PMID: 8504864

DOI: 10.1016/0014-5793(93)81522-2


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