The catalytic property of 3-hydroxyisobutyrate dehydrogenase from bacillus cereus on 3-hydroxypropionate

Tianran Yao; Lin Xu; Hanjie Ying; He Huang; Ming Yan

doi:10.1007/s12010-009-8685-x

The catalytic property of 3-hydroxyisobutyrate dehydrogenase from bacillus cereus on 3-hydroxypropionate

Tianran Yao, Lin Xu, Hanjie Ying, He Huang, Ming Yan

COLLEGE OF BIOTECHNOLOGY AND PHARMACEUTICAL ENGINEERING

Nanjing Tech University

Research output: Contribution to journal › Article › peer-review

17 Scopus citations

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 pH7.0 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.

Original language	English
Pages (from-to)	694-703
Number of pages	10
Journal	Applied Biochemistry and Biotechnology
Volume	160
Issue number	3
DOIs	https://doi.org/10.1007/s12010-009-8685-x
State	Published - Feb 2010

Keywords

3-Hydroxyisobutyrate dehydrogenase
3-Hydroxypropionate
Bacillus cereus

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title = "The catalytic property of 3-hydroxyisobutyrate dehydrogenase from bacillus cereus on 3-hydroxypropionate",

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 pH7.0 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.",

keywords = "3-Hydroxyisobutyrate dehydrogenase, 3-Hydroxypropionate, Bacillus cereus",

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T1 - The catalytic property of 3-hydroxyisobutyrate dehydrogenase from bacillus cereus on 3-hydroxypropionate

AU - Yao, Tianran

AU - Xu, Lin

AU - Ying, Hanjie

AU - Huang, He

AU - Yan, Ming

PY - 2010/2

Y1 - 2010/2

N2 - 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 pH7.0 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.

AB - 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 pH7.0 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.

KW - 3-Hydroxyisobutyrate dehydrogenase

KW - 3-Hydroxypropionate

KW - Bacillus cereus

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The catalytic property of 3-hydroxyisobutyrate dehydrogenase from bacillus cereus on 3-hydroxypropionate

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