RT Journal Article SR Electronic T1 N-Acetyltransferase of Brain: Some Properties of the Enzyme and the Identification of β-Carboline Inhibitor Compounds JF Molecular Pharmacology JO Mol Pharmacol FD American Society for Pharmacology and Experimental Therapeutics SP 69 OP 72 VO 12 IS 1 A1 H.-Y. T. YANG A1 N. H. NEFF YR 1976 UL http://molpharm.aspetjournals.org/content/12/1/69.abstract AB Several β-carboline derivatives, such as harmane, harmol, 6-methoxyharman, and melatonin, inhibited the N-acetylation of tryptamine by brain N-acetyltransferase. The enzyme of brain was active toward several indole- and phenylethylamine substrates. In contrast to the enzyme of brain, the enzyme of pineal was not inhibited by harmaline and harman, and 3,4-dimethoxyphenylethylamine was a relatively poor substrate. β-carboline inhibitors may be useful aids for studying the various N-acetyltransferases and for evaluating the physiological role of the brain enzyme. ACKNOWLEDGMENT We thank Jeffrey Rubenstein for his expert technical assistance.