NADP-dependent phenylacetaldehyde dehydrogenase for degradation of phenylethylamine in Arthrobacter globiformis

We have found that Arthrobacter globiformis IFO 12137 (ATCC 8010) can utilize phenylethylamine (PEA) as a sole carbon and nitrogen source, and we purified PEA oxidase. We have described in the preceding report that this enzyme may be a copper-quinoprotein amine oxidase because of its sensitivity to...

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Veröffentlicht in:Bioscience, biotechnology, and biochemistry biotechnology, and biochemistry, 1993-01, Vol.57 (5), p.852-853
Hauptverfasser: Shimizu, E, Ichise, H, Odawara, T, Yorifuji, T
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Sprache:eng
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Zusammenfassung:We have found that Arthrobacter globiformis IFO 12137 (ATCC 8010) can utilize phenylethylamine (PEA) as a sole carbon and nitrogen source, and we purified PEA oxidase. We have described in the preceding report that this enzyme may be a copper-quinoprotein amine oxidase because of its sensitivity to carbonyl group-blocking reagents and Cu super(2+) chelators. The activity of NADP-dependent dehydrogenation of phenylacetaldehyde (PAAL) has also been detected in extracts of cells grown on PEA. We purified the dehydrogenase partially from the cells of A. globiformis grown on this amine, and confirmed the reaction catalyzed by the enzyme. This paper describes the reaction sequence for the degradation of PEA and some properties of the enzyme from A. globiformis.
ISSN:0916-8451