title: Distribution of amine oxidases and amine dehydrogenases in bacteria grown on primary amines and characterization of the amine oxidase from Klebsiella oxytoca.
abstract: The bacteria Klebsiella oxytoca LMD 72.65 (ATCC 8724), Arthrobacter P1 LMD 81.60 (NCIB 11625), Paracoccus versutus LMD 80.62 (ATCC 25364), Escherichia coli W LMD 50.28 (ATCC 9637), E. coli K12 LMD 93.68, Pseudomonas aeruginosa PAO1 LMD 89.1 (ATCC 17933) and Pseudomonas putida 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 K. oxytoca and E. coli as well as the Gram-positive methylotroph Arthrobacter P1 used an oxidase whereas the pseudomonads and the Gram-negative methylotroph Paracoccus versutus used a dehydrogenase for amine oxidation. K. oxytoca 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 oxidase (EC 1.4.3.6): the molecular mass (172,000 Da) of the homodimeric protein; the UV/visible and EPR spectra of isolated and p-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 K. oxytoca produces a copper-quinoprotein oxidase which is very similar to that found in other Enterobacteriaceae.
authors.affiliation: Department of Microbiology and Enzymology, Delft University of Technology,Julianalaan 67, 2628 BC Delft,The Netherlands.
authors.forename: Ayse
authors.initials: A
authors.lastname: Hacisalihoglu
authors.affiliation: Department of Microbiology and Enzymology, Delft University of Technology,Julianalaan 67, 2628 BC Delft,The Netherlands.
authors.forename: Jaap A
authors.initials: JA
authors.lastname: Jongejan
authors.affiliation: Department of Microbiology and Enzymology, Delft University of Technology,Julianalaan 67, 2628 BC Delft,The Netherlands.
authors.forename: Johannis A
authors.initials: JA
authors.lastname: Duine
mesh_terms: D000588:Amines / Q000378:metabolism*; D000595:Amino Acid Sequence; D003300:Copper / Q000032:analysis; D004295:Dihydroxyphenylalanine / Q000031:analogs & derivatives / Q000032:analysis; D007709:Klebsiella / Q000201:enzymology*; D009682:Magnetic Resonance Spectroscopy; D008667:Metalloproteins / Q000145:classification / Q000302:isolation & purification / Q000378:metabolism*; D008969:Molecular Sequence Data; D000587:Oxidoreductases Acting on CH-NH Group Donors / Q000145:classification / Q000302:isolation & purification / Q000378:metabolism*; D010627:Phenethylamines / Q000378:metabolism; D017421:Sequence Analysis; D017386:Sequence Homology, Amino Acid; D013053:Spectrophotometry; D013347:Subcellular Fractions / Q000201:enzymology
chemical_list: D000588:Amines; D008667:Metalloproteins; D010627:Phenethylamines; C029261:phenethylamine; D004295:Dihydroxyphenylalanine; C067626:6-hydroxydopa quinone; D003300:Copper; D000587:Oxidoreductases Acting on CH-NH Group Donors