Abstract
The open reading frame YLR070c of Saccharomyces cerevisiae has high sequence similarity to S. cerevisiae sorbitol dehydrogenase and to xylitol dehydrogenase of Pichia stipitis. Overexpression of this open reading frame in S. cerevisiae resulted in xylitol dehydrogenase activity. The enzyme is specific for NADH. The following Michaelis constants were estimated: D-xylulose, 1.1 mM; NADH, 240 μM (at pH 7.0); xylitol, 25 mM; NAD, 100 μM (at pH 9.0). Xylitol dehydrogenase activity with the same kinetic properties can also be induced by xylose in wild type S. cerevisiae cells. Copyright (C) 1999 Federation of European Biochemical Societies.
Original language | English |
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Pages (from-to) | 135-138 |
Number of pages | 4 |
Journal | FEBS Letters |
Volume | 457 |
Issue number | 1 |
DOIs | |
Publication status | Published - 20 Aug 1999 |
MoE publication type | A1 Journal article-refereed |
Keywords
- D-Xylulose
- Enzyme kinetics
- Saccharomyces cerevisiae
- Xylitol dehydrogenase
- Xylose metabolism