Purification and characterization of L-2,3-butanediol dehydrogenase of Brevibacterium saccharolyticum C-1012 expressed in Escherichia coli

Biosci Biotechnol Biochem. 2001 Aug;65(8):1876-8. doi: 10.1271/bbb.65.1876.

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

  • Alcohol Oxidoreductases / antagonists & inhibitors
  • Alcohol Oxidoreductases / chemistry*
  • Alcohol Oxidoreductases / isolation & purification
  • Brevibacterium / enzymology*
  • Brevibacterium / genetics
  • Chromatography, Gel
  • Chromatography, High Pressure Liquid
  • Drug Resistance, Microbial
  • Enzyme Inhibitors / pharmacology
  • Escherichia coli / enzymology*
  • Genes, MDR / drug effects
  • Hydrogen-Ion Concentration
  • Isoelectric Focusing
  • Kinetics
  • Metals / chemistry
  • Molecular Weight
  • NAD / metabolism
  • Substrate Specificity

Substances

  • Enzyme Inhibitors
  • Metals
  • NAD
  • Alcohol Oxidoreductases
  • butanediol dehydrogenase