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The Catalytic Property of 3-Hydroxyisobutyrate Dehydrogenase from Bacillus cereus on 3-Hydroxypropionate

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Abstract

The MmsB gene product from Bacillus cereus ATCC14579 exhibits 3-hydroxypropionate dehydrogenase activity. It encodes the 32-kDa enzyme protein composed of 292 amino acids. Recombinant 3-hydroxyisobutyrate dehydrogenase (3-HIBADH) was purified 100-fold from cell extract by ammonium sulfate fractionation and column chromatography. The enzyme catalyzed oxidation of 3-hydroxypropionate (3-HP) between pH 7.0 and 10.0 with optimal activity between 8.8 and 9.0. A Km of 16.8 mM for 3-HP was calculated from a Lineweaver–Burk plot. The semialdehyde as products has been proven by spectrophotometric determination. The dehydrogenase apparently has no metal ion requirement. Kinetic determinations established that 3-HIBADH was more active with NADP+ than NAD+, which did not show similarity with previously reported 3-HIBADH except that from Thermus thermophilus.

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Authors and Affiliations

  1. Nanjing University of Technology, Nanjing, China

    Tianran Yao, Lin Xu, Hanjie Ying & He Huang

  2. College of Biotechnology and Pharmaceutical Engineering, Nanjing University of Technology, Nanjing, China

    Ming Yan

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  1. Tianran Yao
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  2. Lin Xu
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  3. Hanjie Ying
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  4. He Huang
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  5. Ming Yan
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Correspondence to Ming Yan.

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Yao, T., Xu, L., Ying, H. et al. The Catalytic Property of 3-Hydroxyisobutyrate Dehydrogenase from Bacillus cereus on 3-Hydroxypropionate. Appl Biochem Biotechnol 160, 694–703 (2010). https://doi.org/10.1007/s12010-009-8685-x

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  • DOI: https://doi.org/10.1007/s12010-009-8685-x

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