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

• Published in: Yeast (Chichester, England) Vol. 11; no. 9; p. 839
• Main Authors: Hallborn, J, Walfridsson, M, Penttilä, M, Keränen, S, Hahn-Hägerdal, B
• Format: Journal Article
• Language: English
• Published: England 01.07.1995
• Subjects: Amino Acid Sequence; Arabinose - metabolism; Base Sequence; Cloning, Molecular; DNA Primers - genetics; DNA, Complementary - genetics; DNA, Fungal - genetics; Genes, Fungal; Molecular Sequence Data; Pichia - enzymology; Pichia - genetics; Pichia - growth & development; Saccharomyces cerevisiae - genetics; Saccharomyces cerevisiae - growth & development; Saccharomyces cerevisiae - metabolism; Sugar Alcohol Dehydrogenases - genetics; Sugar Alcohol Dehydrogenases - metabolism; Sugar Alcohols - metabolism
• ISSN: 0749-503X
• DOI: 10.1002/yea.320110906

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 lambda-cDNA library with a zymogram technique. D-Arabinitol, xylitol, D-glucitol and galactitol are substrates for the recombinant 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.