Gonzalez E, et al. (2010) Role of Saccharomyces cerevisiae Oxidoreductases Bdh1p and Ara1p in the Metabolism of Acetoin and 2,3-Butanediol. Appl Environ Microbiol 76(3):670-9
Abstract: NAD-dependent butanediol dehydrogenase (Bdh1p) from Saccharomyces cerevisiae reversibly transforms acetoin to 2,3-butanediol in a stereospecific manner. Deletion of BDH1 results in an accumulation of acetoin and a diminution of 2,3-butanediol in two S. cerevisiae strains and two different growth conditions. The concentrations of (2R,3R)-2,3-butanediol are mostly dependent of Bdh1p activity, while those of (meso)-2,3-butanediol are also influenced by the activity of NADP(H)-dependent oxidoreductases. One of them has been purified and shown to be D-Arabinose dehydrogenase (Ara1p), that converts (R/S)-acetoin to meso-2,3-butanediol and (2S,3S)-2,3-butanediol. Deletion of BDH2, an adjacent gene to BDH1, whose encoded protein is 51% identical to Bdh1p, does not alter significatively the levels of acetoin or 2,3-butanediol in comparison to the wild type strain. Furthermore, we have expressed Bdh2p with an histidine tag and shown to be inactive towards 2,3-butanediol. A whole-genome expression analysis with microarrays demonstrates that BDH1 and BDH2 are reciprocally regulated.
|Status: Published||Type: Journal Article||PubMed ID: 19966022|
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