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 Mg2+, Ca2+, and Mn2+. On the other hand, it was inhibited by SH reagents (Hg2+, p-chloromercuribenzoate, iodoacetamide, and N-ethylmaleinimide). The substrate specificity of the enzyme is compared with those of various aldehyde dehydrogenases.
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This research was partially supported by the Ministry of Education, Culture, Sports, Science and Technology, Grant-in-Aid for the 21st century COE Program entitled “Understanding and Control of Life’s Function via Systems Biology”, Keio University. We thank Midori Matsumoto and Hiroyuki Kawahara for N-terminal amino acid sequencing.
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Hirano, J., Miyamoto, K. & Ohta, H. Purification and characterization of aldehyde dehydrogenase with a broad substrate specificity originated from 2-phenylethanol-assimilating Brevibacterium sp. KU1309. Appl Microbiol Biotechnol 76, 357–363 (2007). https://doi.org/10.1007/s00253-007-1004-y
- Aldehyde Dehydrogenase
- Broad Substrate Specificity
- Aliphatic Aldehyde
- Styrene Oxide