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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
2010-1-22
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pubmed:abstractText |
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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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
1559-0291
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:volume |
160
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
694-703
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pubmed:meshHeading |
pubmed-meshheading:19517068-Alcohol Oxidoreductases,
pubmed-meshheading:19517068-Aldehydes,
pubmed-meshheading:19517068-Amino Acid Sequence,
pubmed-meshheading:19517068-Bacillus cereus,
pubmed-meshheading:19517068-Biocatalysis,
pubmed-meshheading:19517068-Cloning, Molecular,
pubmed-meshheading:19517068-Enzyme Stability,
pubmed-meshheading:19517068-Hydrogen-Ion Concentration,
pubmed-meshheading:19517068-Kinetics,
pubmed-meshheading:19517068-Lactic Acid,
pubmed-meshheading:19517068-Metals,
pubmed-meshheading:19517068-Molecular Sequence Data,
pubmed-meshheading:19517068-Spectrophotometry,
pubmed-meshheading:19517068-Substrate Specificity,
pubmed-meshheading:19517068-Temperature,
pubmed-meshheading:19517068-Thiobarbiturates
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pubmed:year |
2010
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pubmed:articleTitle |
The catalytic property of 3-hydroxyisobutyrate dehydrogenase from Bacillus cereus on 3-hydroxypropionate.
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pubmed:affiliation |
Nanjing University of Technology, Nanjing, China.
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pubmed:publicationType |
Journal Article
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