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- Title
The Catalytic Property of 3-Hydroxyisobutyrate Dehydrogenase from Bacillus cereus on 3-Hydroxypropionate.
- Authors
Tianran Yao; Lin Xu; Hanjie Ying; He Huang; Ming Yan
- Abstract
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.
- Subjects
DEHYDROGENASES; BACILLUS cereus; ENZYMES; CATALYSIS; AMINO acids; PROTEINS; AMMONIUM sulfate; CELL separation
- Publication
Applied Biochemistry & Biotechnology, 2010, Vol 160, Issue 3, p694
- ISSN
0273-2289
- Publication type
Academic Journal
- DOI
10.1007/s12010-009-8685-x