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A short‐chain dehydrogenase gene from Pichia stipitis having D ‐arabinitol dehydrogenase activity
Author(s) -
Hallborn Johan,
Walfridsson Mats,
Penttilä Merja,
Keränen Sirkka,
Hahnhägerdal Bärbel
Publication year - 1995
Publication title -
yeast
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.923
H-Index - 102
eISSN - 1097-0061
pISSN - 0749-503X
DOI - 10.1002/yea.320110906
Subject(s) - pichia stipitis , biology , gene , dehydrogenase , yeast , biochemistry , enzyme , microbiology and biotechnology , saccharomyces cerevisiae
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.