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

生物与制药工程学院

Nanjing Tech University

科研成果: 期刊稿件 › 文章 › 同行评审

17 引用（Scopus）

摘要

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.

源语言	英语
页（从-至）	694-703
页数	10
期刊	Applied Biochemistry and Biotechnology
卷	160
期	3
DOI	https://doi.org/10.1007/s12010-009-8685-x
出版状态	已出版 - 2月 2010

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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 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",

author = "Tianran Yao and Lin Xu and Hanjie Ying and He Huang and Ming Yan",

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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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ER -

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

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