Title : On the formation and nature of the imidazoline I2 binding site on human monoamine oxidase-B.

Pub. Date : 2010 Dec

PMID : 20832472






4 Functional Relationships(s)
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1 Incubation of MAO-B with 2-phenylethylamine, an endogenous trace amine and MAO-B substrate, resulted in a progressive loss of enzyme activity, increased enzyme mass, distinct spectral changes and, as was observed with tranylcypromine, a parallel increase in high affinity binding of [(3)H]2-BFI. 2-(2-benzofuranyl)-2-imidazoline monoamine oxidase B Homo sapiens
2 Kinetic studies of the mechanism by which 2-BFI inhibits MAO-B activity suggested binding of 2-BFI, at micromolar concentrations, to a site distinct from the active site on at least two forms of the pure enzyme, probably corresponding to oxidised and reduced enzyme states. 2-(2-benzofuranyl)-2-imidazoline monoamine oxidase B Homo sapiens
3 Kinetic studies of the mechanism by which 2-BFI inhibits MAO-B activity suggested binding of 2-BFI, at micromolar concentrations, to a site distinct from the active site on at least two forms of the pure enzyme, probably corresponding to oxidised and reduced enzyme states. 2-(2-benzofuranyl)-2-imidazoline monoamine oxidase B Homo sapiens
4 Studies with mutant enzymes revealed a pattern of changes consistent with binding of 2-BFI to the substrate entrance channel of human MAO-B. 2-(2-benzofuranyl)-2-imidazoline monoamine oxidase B Homo sapiens