A short‐chain dehydrogenase gene from Pichia stipitis having D‐arabinitol dehydrogenase activity

Johan Hallborn, Mats Walfridsson, Merja Penttilä, Sirkka Keränen, Bärbel Hahn‐hägerdal

Research output: Contribution to journalArticleScientificpeer-review

18 Citations (Scopus)

Abstract

An NAD+‐dependent D‐arabinitol dehydrogenase (polyol dehydrogenase) gene was isolated from Pichia stipitis CBS 6054 and cloned in Saccharomyces cerevisiae. The gene was isolated by screening of a λ‐cDNA library with a zymogram technique. D‐Arabinitol, xylitol, D‐glucitol and galactitol are substrates for the recominant protein. With D‐arabinitol as substrate the reaction product is D‐ribulose. The molecular weight of the native tetramer enzyme is 110 000 Da and the monomer is 30 000 Da. The amino acid sequence is homologous to the short‐chain dehydrogenase family. It is 85·5% identical to a D‐arabinitol dehydrogenase from Candida albicans. The gene in P. stipitis was induced by D‐arabinitol and P. stipitis was able to grow on D‐arabinitol. The physiological role of D‐rabinitol metabolism is discussed.

Original languageEnglish
Pages (from-to)839-847
Number of pages9
JournalYeast
Volume11
Issue number9
DOIs
Publication statusPublished - 1 Jan 1995
MoE publication typeA1 Journal article-refereed

Fingerprint

Pichia
Oxidoreductases
Genes
Galactitol
L-Iditol 2-Dehydrogenase
Xylitol
Amino Acid Sequence Homology
Candida
Substrates
Candida albicans
Reaction products
Gene Library
Metabolism
NAD
Yeast
Saccharomyces cerevisiae
Polyols
Screening
Monomers
Molecular Weight

Keywords

  • arabinitol metabolism
  • ARDH
  • D‐arabinitol dehydrogenase
  • overexpression
  • Pichia stipitis
  • Saccharomyces cerevisiae
  • xylose metabolism
  • yeast
  • zymogram screening

Cite this

Hallborn, Johan ; Walfridsson, Mats ; Penttilä, Merja ; Keränen, Sirkka ; Hahn‐hägerdal, Bärbel. / A short‐chain dehydrogenase gene from Pichia stipitis having D‐arabinitol dehydrogenase activity. In: Yeast. 1995 ; Vol. 11, No. 9. pp. 839-847.
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abstract = "An NAD+‐dependent D‐arabinitol dehydrogenase (polyol dehydrogenase) gene was isolated from Pichia stipitis CBS 6054 and cloned in Saccharomyces cerevisiae. The gene was isolated by screening of a λ‐cDNA library with a zymogram technique. D‐Arabinitol, xylitol, D‐glucitol and galactitol are substrates for the recominant protein. With D‐arabinitol as substrate the reaction product is D‐ribulose. The molecular weight of the native tetramer enzyme is 110 000 Da and the monomer is 30 000 Da. The amino acid sequence is homologous to the short‐chain dehydrogenase family. It is 85·5{\%} identical to a D‐arabinitol dehydrogenase from Candida albicans. The gene in P. stipitis was induced by D‐arabinitol and P. stipitis was able to grow on D‐arabinitol. The physiological role of D‐rabinitol metabolism is discussed.",
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Hallborn, J, Walfridsson, M, Penttilä, M, Keränen, S & Hahn‐hägerdal, B 1995, 'A short‐chain dehydrogenase gene from Pichia stipitis having D‐arabinitol dehydrogenase activity', Yeast, vol. 11, no. 9, pp. 839-847. https://doi.org/10.1002/yea.320110906

A short‐chain dehydrogenase gene from Pichia stipitis having D‐arabinitol dehydrogenase activity. / Hallborn, Johan; Walfridsson, Mats; Penttilä, Merja; Keränen, Sirkka; Hahn‐hägerdal, Bärbel.

In: Yeast, Vol. 11, No. 9, 01.01.1995, p. 839-847.

Research output: Contribution to journalArticleScientificpeer-review

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AU - Hallborn, Johan

AU - Walfridsson, Mats

AU - Penttilä, Merja

AU - Keränen, Sirkka

AU - Hahn‐hägerdal, Bärbel

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AB - An NAD+‐dependent D‐arabinitol dehydrogenase (polyol dehydrogenase) gene was isolated from Pichia stipitis CBS 6054 and cloned in Saccharomyces cerevisiae. The gene was isolated by screening of a λ‐cDNA library with a zymogram technique. D‐Arabinitol, xylitol, D‐glucitol and galactitol are substrates for the recominant protein. With D‐arabinitol as substrate the reaction product is D‐ribulose. The molecular weight of the native tetramer enzyme is 110 000 Da and the monomer is 30 000 Da. The amino acid sequence is homologous to the short‐chain dehydrogenase family. It is 85·5% identical to a D‐arabinitol dehydrogenase from Candida albicans. The gene in P. stipitis was induced by D‐arabinitol and P. stipitis was able to grow on D‐arabinitol. The physiological role of D‐rabinitol metabolism is discussed.

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