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

Bengt Persson, Johan Hallborn, Mats Walfridsson, Bärbel Hahn-Hägerdal, Sirkka Keränen, Merja Penttilä, Hans Jörnvall

Research output: Contribution to journalArticleScientificpeer-review

35 Citations (Scopus)


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 Iγ1 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.

Original languageEnglish
Pages (from-to)9-14
Number of pages6
JournalFEBS Letters
Issue number1
Publication statusPublished - 7 Jun 1993
MoE publication typeA1 Journal article-refereed


  • Active site
  • Enzyme relationship
  • Protein family: Homology
  • Short-chain dehydrogenase: Medium-chain alcohol dehydrogenase

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