Skip to content

Sidney Udenfriend

1 paper in the library · 59 citations · publishing 1962

Papers

Studies on the Mechanism of Action of Monoamine Oxidase: Metabolism of N,N-Dimethyltryptamine and N,N-Dimethyltryptamine-N-Oxide

Biochemistry January 1, 1962 Thomas E. Smith, Herbert Weissbach, Sidney Udenfriend 59 citations

Monoamine oxidase (MAO) catalyzes the conversion of N,N-dimethyltryptamine (DMT) to its N-oxide form, N,N-dimethyltryptamine-N-oxide, and the reaction mechanism involves oxidative deamination. The enzyme's action on DMT proceeds through a pathway that includes the formation of an intermediate imine, which is then hydrolyzed to yield the final product. The study demonstrates that DMT-N-oxide is not a direct substrate for MAO but can be reduced back to DMT by other enzymatic systems, suggesting a potential regulatory cycle for DMT levels in tissues.