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Appl Microbiol Biotechnol. 2007 Aug;76(2):357-63. Epub 2007 Jul 7.

Purification and characterization of aldehyde dehydrogenase with a broad substrate specificity originated from 2-phenylethanol-assimilating Brevibacterium sp. KU1309.

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Department of Biosciences and Informatics, Center for Bioscience and Informatics, Keio University, 3-14-1 Hiyoshi, Yokohama 223-8522, Japan.


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.

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