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Enzymatic synthesis of N‐methylhistamine labeled with deuterium and tritium
Author(s) -
Šamonina J.,
Kańska M.
Publication year - 2009
Publication title -
journal of labelled compounds and radiopharmaceuticals
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.432
H-Index - 47
eISSN - 1099-1344
pISSN - 0362-4803
DOI - 10.1002/jlcr.1611
Subject(s) - chemistry , isotopomers , tritium , decarboxylation , deuterium , enzyme , stereochemistry , radiochemistry , biochemistry , organic chemistry , catalysis , physics , quantum mechanics , molecule , nuclear physics
The isotopomers of N π ‐methylhistamine (πMeHA) and N τ ‐methylhistamine (τMeHA) labeled with deuterium and tritium at the α‐carbon atom of the side chain were obtained using the enzyme histidine decarboxylase (HDC, EC 4.1.1.22) from Lactobacillus 30a. The deuterium labeled isotopomers [(αR)‐ 2 H]‐πMeHA and [(αR)‐ 2 H]‐τMeHA were synthesized by enzymatic decarboxylation of N π ‐methyl‐, and N τ ‐methyl‐ L ‐histidines (respectively) in a fully deuteriated incubation medium. The same decarboxylation carried out in a tritiated medium resulted in tritiated [αR‐ 3 H]‐πMeHA and [αR‐ 3 H]‐τMeHA isotopomers of N‐methylhistamine. Copyright © 2009 John Wiley & Sons, Ltd.