1887

Abstract

The bacteria LMD 72.65 (ATCC 8724), P1 LMD 81.60 (NCIB 11625), LMD 80.62 (ATCC 25364), W LMD 50.28 (ATCC 9637), K12 LMD 93.68, PAO1 LMD 89.1 (ATCC 17933) and LMD 68.20 (ATCC 12633) utilized primary amines as a carbon and energy source, although the range of amines accepted varied from organism to organism. The Gram-negative bacteria and as well as the Gram-positive methylotroph P1 used an oxidase whereas the pseudomonads and the Gram-negative methylotroph used a dehydrogenase for amine oxidation. utilized several primary amines but showed a preference for those containing a phenyl group moiety. Only a single oxidase was used for oxidation of the amines. After purification, the following characteristics of the enzyme indicated that it belonged to the group of copper-quinoprotein amine oxidases (EC 1.4.3.6): the molecular mass (172000 Da) of the homodimeric protein; the UV/visible and EPR spectra of isolated and -nitrophenylhydrazine-inhibited enzyme; the presence and the content of copper and topaquinone (TPQ). The amine oxidase appeared to be soluble and localized in the periplasm, but catalase and NAD-dependent aromatic aldehyde dehydrogenase, enzymes catalysing the conversion of its reaction products, were found in the cytoplasm. From the amino acid sequence of the N-terminal part as well as that of a purified peptide, it appears that produces a copper-quinoprotein oxidase which is very similar to that found in other

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/content/journal/micro/10.1099/00221287-143-2-505
1997-02-01
2019-08-24
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