Purification and characterization of aldehyde dehydrogenase with a broad substrate specificity originated from 2-phenylethanol-assimilating Brevibacterium sp. KU1309.
Phenylacetaldehyde dehydrogenase (PADH) was purified and characterized from Brevibacterium sp. KU1309, which can grow on the medium containing 2-phenylethanol as the sole carbon source. This enzyme was a homotetrameric protein with a subunit of 61 kDa. The enzyme catalyzed the oxidation of aryl (benzaldehyde, phenylacetaldehyde, 3-phenylpropionaldehyde) and aliphatic (hexanal, octanal, decanal) aldehydes to the corresponding carboxylic acids using NAD(+) as the electron acceptor. The PADH activity was enhanced by several divalent cationic ions such as Mg(2+), Ca(2+), and Mn(2+). On the other hand, it was inhibited by SH reagents (Hg(2+), p-chloromercuribenzoate, iodoacetamide, and N-ethylmaleinimide). The substrate specificity of the enzyme is compared with those of various aldehyde dehydrogenases.
Hirano
Jun-ichiro
J
Department of Biosciences and Informatics, Center for Bioscience and Informatics, Keio University, 3-14-1 Hiyoshi, Yokohama 223-8522, Japan.
Miyamoto
Kenji
K
Ohta
Hiromichi
H
D000444:Aldehyde Dehydrogenase / Q000302:isolation & purification*; D000445:Aldehyde Oxidoreductases / Q000302:isolation & purification*; D000447:Aldehydes / Q000378:metabolism; D001951:Brevibacterium / Q000201:enzymology* / Q000378:metabolism; D029968:Escherichia coli Proteins; D006863:Hydrogen-Ion Concentration; D009243:NAD / Q000378:metabolism; D010626:Phenylethyl Alcohol / Q000737:chemistry* / Q000378:metabolism*; D013379:Substrate Specificity
D000447:Aldehydes; D029968:Escherichia coli Proteins; D009243:NAD; D000445:Aldehyde Oxidoreductases; D000444:Aldehyde Dehydrogenase; C053855:phenylacetaldehyde dehydrogenase; D010626:Phenylethyl Alcohol