Copper amine oxidase: cunning cofactor and controversial copper.
Copper amine oxidases have a complex reaction cycle that converts a primary amine and molecular oxygen into the aldehyde, ammonia and hydrogen peroxide. Coupling structural studies of freeze-trapped reaction intermediates in crystals with kinetic and spectroscopic experiments in solution has generated a detailed molecular picture of catalysis. Although dioxygen has been directly observed bound to the copper at a late stage in the reaction cycle, whether copper is the initial binding site remains controversial.
Dawkes
H C
HC
Astbury Centre for Structural Molecular Biology, School of Biochemistry and Molecular Biology, University of Leeds, LS29JT, Leeds, UK.
Phillips
S E
SE
D006631:Amine Oxidase (Copper-Containing) / Q000737:chemistry / Q000378:metabolism*; D019943:Amino Acid Substitution; D000818:Animals; D001665:Binding Sites; D002384:Catalysis; D003067:Coenzymes / Q000378:metabolism; D003300:Copper / Q000378:metabolism; D004295:Dihydroxyphenylalanine / Q000031:analogs & derivatives* / Q000096:biosynthesis; D010084:Oxidation-Reduction; D011487:Protein Conformation
C086758:2,4,5-trihydroxyphenylalanine quinone; D003067:Coenzymes; D004295:Dihydroxyphenylalanine; D003300:Copper; D006631:Amine Oxidase (Copper-Containing)