Affiliation:
1. Department of Chemistry, University of Warsaw, 1 Pasteura Str., 02-093 Warsaw, Poland, Tel.: +48 22 822 0211 ext. 509, Fax: +48 22 822 0211 ext. 434
Abstract
Abstract
The enzymatic deamination of 5-fl uorotryptamine and 5-hydroxytryptamine, 5-HT, catalysed by enzyme monoamine oxidase A (MAO-A, EC 1.4.3.4) was investigated using the kinetic (KIE) and solvent (SIE) isotope effects methods. The numerical values of deuterium isotope effects in the (1R) positions of 5-F-tryptamine were determined using non-competitive spectrophotomeric method. Isotopologue 5-F-[(1R)- -2H]-tryptamine, needed for kinetic studies was obtained by enzymatic decarboxylation of 5´-fl uoro-L-tryptophan, 5´-F-L-Trp, in fully deuteriated medium.
Subject
Waste Management and Disposal,Condensed Matter Physics,Safety, Risk, Reliability and Quality,Instrumentation,Nuclear Energy and Engineering,Nuclear and High Energy Physics
Cited by
3 articles.
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