Studies on the Enzymic Methylation of Histamine.
- 1 January 1964
- journal article
- research article
- Published by Danish Chemical Society in Acta Chemica Scandinavica
- Vol. 18 (9) , 2069-2076
- https://doi.org/10.3891/acta.chem.scand.18-2069
Abstract
The enzymic methylation of histamine has been studied by using an essentially homogeneous preparation of histamine-N-methyl-transferase. The enzyme did not appear to be a metalloenzyme, and no cofactors related to vitamin B12 could be detected in the enzyme preparation. The transferase has SH-groups essential for its enzymic activity, and the pH-optimum of the reaction is 8.8. The influence of some histamine analogues on the reaction as well as studies on substrate specificity are described. The methyl group transfer from S-adenosyl-methionine to histamine probably occurs without a methylated enzyme as an intermediate.This publication has 2 references indexed in Scilit:
- Improved procedure for the isolation of S-adenosylmethionine and S-adenosylethionineArchives of Biochemistry and Biophysics, 1959
- Catabolism of Physiological Quantities of Histamine in VivoPhysiological Reviews, 1959