Catalytic aerobic deamination of activated primary amines by a model for the quinone cofactor of mammalian copper amine oxidases.
Department of Chemistry, Case Western Reserve University, Cleveland, Ohio 44106, USA.
L M
LM
Sayre
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Lee
D000332:Aerobiosis; D006631:Amine Oxidase (Copper-Containing) / Q000737:chemistry* / Q000378:metabolism*; D000818:Animals; D016227:Benzoquinones / Q000138:chemical synthesis / Q000737:chemistry / Q000378:metabolism*; D001596:Benzylamines / Q000378:metabolism; D002384:Catalysis; D003641:Deamination; D004295:Dihydroxyphenylalanine / Q000031:analogs & derivatives* / Q000737:chemistry / Q000378:metabolism; D007202:Indicators and Reagents; D007700:Kinetics; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D008322:Mammals; D008956:Models, Chemical; D010084:Oxidation-Reduction; D012545:Schiff Bases; D013379:Substrate Specificity
D016227:Benzoquinones; D001596:Benzylamines; D007202:Indicators and Reagents; D012545:Schiff Bases; C067344:2,5-di-tert-butylbenzoquinone; D004295:Dihydroxyphenylalanine; C067626:6-hydroxydopa quinone; D006631:Amine Oxidase (Copper-Containing)