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Number of results

Journal

2014 | 59 | 3 | 91-95

Article title

Enzymatic oxidation of substituted tryptamines catalysed by monoamine oxidase

Content

Title variants

Languages of publication

EN

Abstracts

EN
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.

Publisher

Journal

Year

Volume

59

Issue

3

Pages

91-95

Physical description

Dates

published
1 - 8 - 2014
received
1 - 3 - 2013
online
12 - 9 - 2014
accepted
26 - 6 - 2014

Contributors

  • 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
  • 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

References

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Document Type

Publication order reference

Identifiers

YADDA identifier

bwmeta1.element.-psjd-doi-10_2478_nuka-2014-0015
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