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Reference: 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

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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.

Reference Type
Journal Article
Authors
Gonzalez E, Fernandez MR, Marco D, Calam E, Sumoy L, Pares X, Dequin S, Biosca JA
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