Identification and characterization of a mycobacterial (2R,3R)-2,3-butanediol dehydrogenase |
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Authors: | Takeda Minoru Muranushi Takahiro Inagaki Sawako Nakao Takuya Motomatsu Shigekazu Suzuki Ichiro Koizumi Jun-ichi |
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Institution: | Division of Materials Science and Chemical Engineering, Graduate School of Engineering, Yokohama National University, Japan. mtake@ynu.ac.jp |
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Abstract: | Bacterial strain B-009, capable of using racemic 1,2-propanediol (PD), was identified as a rapid-growing member of the genus Mycobacterium. The strain is phylogenetically related to M. gilvum, but has slightly different physiological characteristics. An NAD(+)-dependent enantioselective alcohol dehydrogenase, which acts on R-PD, was purified from the strain. The enzyme was a homodimer of a peptide coded by a 1047-bp gene (mbd1). A highly conserved sequence for medium-chain dehydrogenase/reductases with a preference for secondary alcohols was found in the gene. Hydroxyacetone was produced from R-PD by an enzymatic reaction, indicating that position 2 of the substrate was oxidized. The enzyme activity was highest for (2R,3R)-2,3-butanediol (R,R-BD), enabling the enzyme to be identified as (2R,3R)-2,3-butanediol dehydrogenase (R,R-BD-DH). A homology search revealed M. gilvum, M. vanbaalenii, and M. semegmatis to have ORFs similar to mbd1, suggesting the widespread distribution of genes encoding R,R-BD-DH among mycobacterial strains. |
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