Evidence for copper and 3,4,6-trihydroxyphenylalanine quinone cofactors in an amine oxidase from the gram-negative bacterium Escherichia coli K-12.
The cofactors present in a amine oxidase induced in Escherichia coli K-12 by growth on 2-phenylethylamine have been studied by spectroscopic methods. E.s.r. spectroscopy establishes the presence of cupric copper while resonance Raman spectroscopy on the phenylhydrazine derivative of the enzyme provides strong evidence for the oxidized form of 3,4,6-trihydroxyphenylalanine (TOPA) quinone. The amine oxidase should accordingly be classified as EC 1.4.3.6. This is the first report of such an amine oxidase in a Gram-negative bacterium.
Cooper
R A
RA
Bichemistry Department, University of Leicester, U.K.
Knowles
P F
PF
Brown
D E
DE
McGuirl
M A
MA
Dooley
D M
DM
D006631:Amine Oxidase (Copper-Containing); D003300:Copper / Q000378:metabolism*; D004295:Dihydroxyphenylalanine / Q000031:analogs & derivatives* / Q000378:metabolism; D004578:Electron Spin Resonance Spectroscopy; D004926:Escherichia coli / Q000201:enzymology*; D000587:Oxidoreductases Acting on CH-NH Group Donors / Q000737:chemistry*; D010627:Phenethylamines / Q000378:metabolism; D013057:Spectrum Analysis; D013059:Spectrum Analysis, Raman
D010627:Phenethylamines; C029261:phenethylamine; D004295:Dihydroxyphenylalanine; C067626:6-hydroxydopa quinone; D003300:Copper; D006631:Amine Oxidase (Copper-Containing); D000587:Oxidoreductases Acting on CH-NH Group Donors