Purification and characterization of the alcohol dehydrogenase with a broad substrate specificity originated from 2-phenylethanol-assimilating Brevibacterium sp. KU 1309.
A novel 2-phenylethanol dehydrogenase has been purified from a soil bacterium Brevibacterium sp. KU 1309. The enzyme was purified about 1400-fold to homogeneity, and found to be a monomeric enzyme of apparent 39 kDa. The enzyme had broad substrate specificity and catalyzes a reversible oxidation of various primary alcohols to aldehydes. The enzyme required NAD+, but not NADP+ as a cofactor. Thus, the enzyme was classified into a group of NAD+-dependent primary alcohol dehydrogenase. The activity was inhibited by Cu2+, Ni2+, Ba2+, Hg2+ and p-chloromercuribenzoate. The enzyme is expected to be applicable as an effective biocatalyst in the oxidation of various alcohols.
Hirano
Jun-ichiro
J
Department of Biosciences and Informatics, Center for Biosciences and Informatics, Keio University, 3-14-1 Hiyoshi, Yokohama 223-8522, Japan.
Miyamoto
Kenji
K
Ohta
Hiromichi
H
D000426:Alcohol Dehydrogenase / Q000037:antagonists & inhibitors / Q000737:chemistry* / Q000302:isolation & purification; D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000037:antagonists & inhibitors / Q000737:chemistry* / Q000302:isolation & purification; D001951:Brevibacterium / Q000201:enzymology*; D004791:Enzyme Inhibitors / Q000494:pharmacology; D006863:Hydrogen-Ion Concentration; D007477:Ions / Q000494:pharmacology; D008670:Metals / Q000494:pharmacology; D008969:Molecular Sequence Data; D010626:Phenylethyl Alcohol / Q000378:metabolism*; D013379:Substrate Specificity; D013696:Temperature
D001426:Bacterial Proteins; D004791:Enzyme Inhibitors; D007477:Ions; D008670:Metals; D000426:Alcohol Dehydrogenase; D010626:Phenylethyl Alcohol