[Multiplicity of mitochondrial monoamine exidases and ways of selective blocking of the enzyme activity].
Problems on multiple forms of mitochondrial monoamine oxidases are considered. Possible nature of monoamine oxidase isoenzymes and its A and B forms is discussed. Substrates specificity of mitochondrial monoamine oxidase and the importance of amine chemical structure for the enzyme activity is examined. The data on the structure of mitochondrial monoamine oxidase active center and the presence in it of several regions responsible for amine binding are analyzed. The nature of these regions is discussed. New approaches to selective blocking of the activity of mitochondrial monoamine oxidase are considered on the basis of the hypothesis given on the mechanism of substrate and inhibitor interaction with the enzyme.
D000818:Animals; D001665:Binding Sites; D001679:Biogenic Amines / Q000096:biosynthesis; D003641:Deamination; D006912:Hydroxyquinolines / Q000494:pharmacology*; D007527:Isoenzymes / Q000378:metabolism*; D008930:Mitochondria, Liver / Q000201:enzymology*; D008995:Monoamine Oxidase / Q000378:metabolism*; D008996:Monoamine Oxidase Inhibitors / Q000494:pharmacology*; D009284:Naphthols / Q000494:pharmacology*; D015125:Oxyquinoline / Q000494:pharmacology*; D010627:Phenethylamines; D051381:Rats; D013552:Swine
D001679:Biogenic Amines; D006912:Hydroxyquinolines; D007527:Isoenzymes; D008996:Monoamine Oxidase Inhibitors; D009284:Naphthols; D010627:Phenethylamines; D015125:Oxyquinoline; D008995:Monoamine Oxidase
O mnozhestvennosti mitokhondrial'nykh monoaminoksidaz i putiakh izbiratel'nogo blokirovaniia aktivnosti fermenta.