Abstract
THE in vivo studies of Schayer1 have shown ring N-methylation to be the principal pathway of histamine metabolism in a variety of mammalian species. His work demonstrates the following scheme: Kobayashi2 found that incubation of histamine with whole-liver homogenates resulted in the formation of 1-methylimidazole-4-acetic acid. These observations reflect the summation of at least three enzymatic processes, one of which is concerned with the synthesis of a co-factor needed for histamine methylation. This report describes the isolation and properties of an enzyme, imidazole N-methyl transferase, which catalyses the ring-N-methylation of histamine requiring S-adenosylmethionine as the methyl donor. © 1959 Nature Publishing Group.
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CITATION STYLE
Brown, D. D., Axelrod, J., & Tomchick, R. (1959). Enzymatic n-methylation of histamine. Nature, 183(4662), 680. https://doi.org/10.1038/183680a0
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