The Catalytic Property of 3-Hydroxyisobutyrate Dehydrogenase from Bacillus cereus on 3-Hydroxypropionate |
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| Authors: | Tianran Yao Lin Xu Hanjie Ying He Huang Ming Yan |
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| Institution: | 1. Nanjing University of Technology, Nanjing, China
2. College of Biotechnology and Pharmaceutical Engineering, Nanjing University of Technology, Nanjing, China
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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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