Abstract
The L-2,3-butanediol dehydrogenase produced in E. coli JM109/pLBD2-CTC was purified by 5 steps. The molecular mass of this enzyme was estimated at 110 kDa and the subunit was measured to be 30 kDa. The L-BDH had some differences from the BDHs from other sources in substrate specificity, pI value, pH stability, effects of divalent cations, and organic acids.
MeSH terms
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Alcohol Oxidoreductases / antagonists & inhibitors
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Alcohol Oxidoreductases / chemistry*
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Alcohol Oxidoreductases / isolation & purification
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Brevibacterium / enzymology*
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Brevibacterium / genetics
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Chromatography, Gel
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Chromatography, High Pressure Liquid
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Drug Resistance, Microbial
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Enzyme Inhibitors / pharmacology
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Escherichia coli / enzymology*
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Genes, MDR / drug effects
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Hydrogen-Ion Concentration
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Isoelectric Focusing
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Kinetics
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Metals / chemistry
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Molecular Weight
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NAD / metabolism
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Substrate Specificity
Substances
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Enzyme Inhibitors
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Metals
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NAD
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Alcohol Oxidoreductases
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butanediol dehydrogenase