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-arabinitol metabolism is discussed.

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

Keywords

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

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