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.
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References
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BROWN, D., AXELROD, J. & TOMCHICK, R. Enzymatic N-Methylation of Histamine. Nature 183, 680 (1959). https://doi.org/10.1038/183680a0
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DOI: https://doi.org/10.1038/183680a0
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