Studies on the Mechanism of Action of Monoamine Oxidase: Metabolism of N,N-Dimethyltryptamine and N,N-Dimethyltryptamine-N-Oxide
Thomas E. Smith, Herbert Weissbach, Sidney Udenfriend
Biochemistry January 1, 1962 DOI: 10.1021/bi00907a021 via OpenAlex
Summary
AI-generated from the abstractMonoamine 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.
Study at a glance
| Characteristics | Experimental study Peer reviewed |
|---|---|
| Keywords | Computer science Monoamine oxidase Citation database Information retrieval Library science |
| Citations | 59 |
| Key finding | Monoamine oxidase metabolizes N,N-dimethyltryptamine via oxidative deamination, and the resulting N-oxide can be reduced back to DMT by other enzymes. |
Abstract
ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTStudies on the Mechanism of Action of Monoamine Oxidase: Metabolism of N,N-Dimethyltryptamine and N,N-Dimethyltryptamine-N-OxideT. E. Smith, H. Weissbach, and S. UdenfriendCite this: Biochemistry 1962, 1, 1, 137–143Publication Date (Print):January 1, 1962Publication History Published online1 May 2002Published inissue 1 January 1962https://doi.org/10.1021/bi00907a021Request reuse permissionsArticle Views354Altmetric-Citations51LEARN ABOUT THESE METRICSArticle Views are the COUNTER-compliant sum of full text article downloads since November 2008 (both PDF and HTML) across all institutions and individuals. These metrics are regularly updated to reflect usage leading up to the last few days.Citations are the number of other articles citing this article, calculated by Crossref and updated daily. Find more information about Crossref citation counts.The Altmetric Attention Score is a quantitative measure of the attention that a research article has received online. Clicking on the donut icon will load a page at altmetric.com with additional details about the score and the social media presence for the given article. Find more information on the Altmetric Attention Score and how the score is calculated. Share Add toView InAdd Full Text with ReferenceAdd Description ExportRISCitationCitation and abstractCitation and referencesMore Options Share onFacebookTwitterWechatLinked InReddit PDF (780 KB) Get e-Alertsclose Get e-Alerts