Pineal N-acetyltransferase is inactivated by disulfide-containing peptides: insulin is the most potent.
Pineal N-acetyltransferase can be inactivated in broken cell preparations by cystamine through a mechanism of thiol-disulfide exchange. Some, but not all, disulfide-containing peptides can inactivate this enzyme; the most potent inactivator is insulin. These findings suggest that a disulfide-containing peptide with high reactivity toward N-acetyltransferase may participate in the intracellular regulation of this enzyme.
D000123:Acetyltransferases / Q000037:antagonists & inhibitors*; D000818:Animals; D004220:Disulfides / Q000494:pharmacology; D004229:Dithiothreitol / Q000494:pharmacology; D006728:Hormones / Q000494:pharmacology; D006863:Hydrogen-Ion Concentration; D007328:Insulin / Q000494:pharmacology*; D007700:Kinetics; D008297:Male; D010455:Peptides / Q000494:pharmacology*; D010870:Pineal Gland / Q000201:enzymology*; D051381:Rats; D013329:Structure-Activity Relationship
D004220:Disulfides; D006728:Hormones; D007328:Insulin; D010455:Peptides; D000123:Acetyltransferases; D004229:Dithiothreitol