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 transf...
This chapter discusses the redox properties of the flavin cofactor of monoamine oxidases (MAO) A and...
This chapter discusses the redox properties of the flavin cofactor of monoamine oxidases (MAO) A and...
The structural details of the interactions of the covalent 8alpha-S-cysteinyl-FAD with the protein m...
Due to their pharmacological importance in the oxidation of amine neurotransmitters, the membrane-bo...
The mechanism of amine oxidation by flavoprotein enzymes is critically analysed through analysis of ...
tMonoamine oxidase (MAO) enzymes regulate the level of neurotransmitters by catalyzing the oxidation...
The flavin-containing enzyme monoamine oxidase (MAO) is essential for the enzymatic decomposition of...
The flavin-containing enzyme monoamine oxidase (MAO) is essential for the enzymatic decomposition of...
Although a considerable amount of mechanistic data has accumulated in literature, the detailed mecha...
The flavoenzyme monoamine oxidase (MAO) is essential for the enzymatic decomposition of neurotransmi...
The flavoenzyme monoamine oxidase (MAO) is essential for the enzymatic decomposition of neurotransmi...
The flavoenzyme monoamine oxidase (MAO) plays a crucial role in regulating animal behavioural patter...
Current structural results of several flavin-dependent amine oxidizing enzymes including human monoa...
Current structural results of several flavin-dependent amine oxidizing enzymes including human monoa...
This chapter discusses the redox properties of the flavin cofactor of monoamine oxidases (MAO) A and...
This chapter discusses the redox properties of the flavin cofactor of monoamine oxidases (MAO) A and...
This chapter discusses the redox properties of the flavin cofactor of monoamine oxidases (MAO) A and...
The structural details of the interactions of the covalent 8alpha-S-cysteinyl-FAD with the protein m...
Due to their pharmacological importance in the oxidation of amine neurotransmitters, the membrane-bo...
The mechanism of amine oxidation by flavoprotein enzymes is critically analysed through analysis of ...
tMonoamine oxidase (MAO) enzymes regulate the level of neurotransmitters by catalyzing the oxidation...
The flavin-containing enzyme monoamine oxidase (MAO) is essential for the enzymatic decomposition of...
The flavin-containing enzyme monoamine oxidase (MAO) is essential for the enzymatic decomposition of...
Although a considerable amount of mechanistic data has accumulated in literature, the detailed mecha...
The flavoenzyme monoamine oxidase (MAO) is essential for the enzymatic decomposition of neurotransmi...
The flavoenzyme monoamine oxidase (MAO) is essential for the enzymatic decomposition of neurotransmi...
The flavoenzyme monoamine oxidase (MAO) plays a crucial role in regulating animal behavioural patter...
Current structural results of several flavin-dependent amine oxidizing enzymes including human monoa...
Current structural results of several flavin-dependent amine oxidizing enzymes including human monoa...
This chapter discusses the redox properties of the flavin cofactor of monoamine oxidases (MAO) A and...
This chapter discusses the redox properties of the flavin cofactor of monoamine oxidases (MAO) A and...
This chapter discusses the redox properties of the flavin cofactor of monoamine oxidases (MAO) A and...
The structural details of the interactions of the covalent 8alpha-S-cysteinyl-FAD with the protein m...