Structural insights into the mechanism of amine oxidation by monoamine oxidases A and B.
Due to their pharmacological importance in the oxidation of amine neurotransmitters, the membrane-bound flavoenzymes monoamine oxidase A and monoamine oxidase B have attracted numerous investigations and, as a result, two different mechanisms; the single electron transfer and the polar nucleophilic mechanisms, have been proposed to describe their catalytic mechanisms. This review compiles the recently available structural data on both enzymes with available mechanistic data as well as current NMR data on flavin systems to provide an integration of the approaches. These conclusions support the proposal that a polar nucleophilic mechanism for amine oxidation is the most consistent mechanistic scheme as compared with the single electron transfer mechanism.
Edmondson
Dale E
DE
Departments of Biochemistry and Chemistry, Emory University, 1510 Clifton Road, Atlanta, GA 30322, USA. deedmon@emory.edu
Binda
Claudia
C
Mattevi
Andrea
A
D000588:Amines / Q000737:chemistry*; D001665:Binding Sites; D002384:Catalysis; D003198:Computer Simulation; D004789:Enzyme Activation; D008956:Models, Chemical; D008958:Models, Molecular; D008995:Monoamine Oxidase / Q000737:chemistry*; D010084:Oxidation-Reduction; D011485:Protein Binding; D011487:Protein Conformation; D013329:Structure-Activity Relationship
D000588:Amines; D008995:Monoamine Oxidase