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)

Abstract

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
Volume324
Issue number1
DOIs
Publication statusPublished - 7 Jun 1993
MoE publication typeA1 Journal article-refereed

Fingerprint

D-Xylulose Reductase
Alcohol Dehydrogenase
L-Iditol 2-Dehydrogenase
L-threonine 3-dehydrogenase
Proteins
Enzymes
Genes
Pichia
Sorbitol
Enzyme activity
Yeast
Structural properties
Oxidoreductases
Yeasts

Keywords

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

Cite this

Persson, B., Hallborn, J., Walfridsson, M., Hahn-Hägerdal, B., Keränen, S., Penttilä, M., & Jörnvall, H. (1993). Dual relationships of xylitol and alcohol dehydrogenases in families of two protein types. FEBS Letters, 324(1), 9-14. https://doi.org/10.1016/0014-5793(93)81522-2
Persson, Bengt ; Hallborn, Johan ; Walfridsson, Mats ; Hahn-Hägerdal, Bärbel ; Keränen, Sirkka ; Penttilä, Merja ; Jörnvall, Hans. / Dual relationships of xylitol and alcohol dehydrogenases in families of two protein types. In: FEBS Letters. 1993 ; Vol. 324, No. 1. pp. 9-14.
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Persson, B, Hallborn, J, Walfridsson, M, Hahn-Hägerdal, B, Keränen, S, Penttilä, M & Jörnvall, H 1993, 'Dual relationships of xylitol and alcohol dehydrogenases in families of two protein types', FEBS Letters, vol. 324, no. 1, pp. 9-14. https://doi.org/10.1016/0014-5793(93)81522-2

Dual relationships of xylitol and alcohol dehydrogenases in families of two protein types. / Persson, Bengt; Hallborn, Johan; Walfridsson, Mats; Hahn-Hägerdal, Bärbel; Keränen, Sirkka; Penttilä, Merja; Jörnvall, Hans.

In: FEBS Letters, Vol. 324, No. 1, 07.06.1993, p. 9-14.

Research output: Contribution to journalArticleScientificpeer-review

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AU - Persson, Bengt

AU - Hallborn, Johan

AU - Walfridsson, Mats

AU - Hahn-Hägerdal, Bärbel

AU - Keränen, Sirkka

AU - Penttilä, Merja

AU - Jörnvall, Hans

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AB - 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.

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