Purification and characterization of L-2,3-butanediol dehydrogenase of Brevibacterium saccharolyticum C-1012 expressed in Escherichia coli.
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.
Takusagawa
Y
Y
Department of Applied Chemistry and Biotechnology, Faculty of Engineering, Yamanashi University, Kofu, Japan. g98ds006@ccn.yamanashi.ac.jp
Otagiri
M
M
Ui
S
S
Ohtsuki
T
T
Mimura
A
A
Ohkuma
M
M
Kudo
T
T
D000429:Alcohol Oxidoreductases / Q000037:antagonists & inhibitors / Q000737:chemistry* / Q000302:isolation & purification; D001951:Brevibacterium / Q000201:enzymology* / Q000235:genetics; D002850:Chromatography, Gel; D002851:Chromatography, High Pressure Liquid; D004352:Drug Resistance, Microbial; D004791:Enzyme Inhibitors / Q000494:pharmacology; D004926:Escherichia coli / Q000201:enzymology*; D019450:Genes, MDR / Q000187:drug effects; D006863:Hydrogen-Ion Concentration; D007525:Isoelectric Focusing; D007700:Kinetics; D008670:Metals / Q000737:chemistry; D008970:Molecular Weight; D009243:NAD / Q000378:metabolism; D013379:Substrate Specificity
D004791:Enzyme Inhibitors; D008670:Metals; D009243:NAD; D000429:Alcohol Oxidoreductases; C019801:butanediol dehydrogenase