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The Enzymatic -N-Methylation of Histidine

From the ¹ From the Department of Biochemistry, University of Vermont College of Medicine, Burlington, Vermont 05401

Cell-free extracts of Neurospora crassa catalyze the methylation of the -amino nitrogen atom of histidine, -N-methylhistidine, and -N,N-dimethylhistidine to form hercynine (-N,N,N-trimethylhistidine). S-Adenosylmethionine serves as the common methyl group donor. The enzyme system responsible for these methylations has been purified 500-fold by DEAE-cellulose chromatography, ammonium sulfate fractionation, gel filtration, and DEAE-Sephadex chromatography. The most highly purified preparation showed a single major component during acrylamide gel electrophoresis. Fractionation studies, kinetic studies, inhibition studies, and heat-inactivation studies all indicate that a single enzyme (histidine--N-methyltransferase) is responsible for the three transmethylation reactions involved in the conversion of histidine to hercynine.

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