When monoamine oxidase B (MAO B) from rat liver mitochondria was incubated with MPTP, methylamine was formed and MAO B was inactivated. Incubation of 1-methyl-4-phenyl-2,3-dihydropyridinium (MPDP+) with MAO B also yielded methylamine and resulted in inactivation of the enzyme. Similar rate consts. for inactivation of MAO B were obtained with 1-methyl-4-phenyl-1,4-dihydropyridine, 3-phenylglutaraldehyde (3-PG), and 2,6-dihydroxy-4-phenyltetrahydropyran, suggesting that bioalkylation of the enzyme occurs outside the active site via a species such as 3-PG.
Mechanistic studies on the MPTP inactivation of MAO B / N. Castagnoli, A. Sparatore, S. Ottoboni, L. Leung, A. Trevor. - In: INTERNATIONAL CONGRESS SERIES. - ISSN 0531-5131. - 750 (Pharmacology):(1987), pp. 875-878.
Mechanistic studies on the MPTP inactivation of MAO B
A. SparatoreSecondo
;
1987
Abstract
When monoamine oxidase B (MAO B) from rat liver mitochondria was incubated with MPTP, methylamine was formed and MAO B was inactivated. Incubation of 1-methyl-4-phenyl-2,3-dihydropyridinium (MPDP+) with MAO B also yielded methylamine and resulted in inactivation of the enzyme. Similar rate consts. for inactivation of MAO B were obtained with 1-methyl-4-phenyl-1,4-dihydropyridine, 3-phenylglutaraldehyde (3-PG), and 2,6-dihydroxy-4-phenyltetrahydropyran, suggesting that bioalkylation of the enzyme occurs outside the active site via a species such as 3-PG.Pubblicazioni consigliate
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