The effects of ligands on enzymic carboxyl-methylation of neurophysins.
The methyl-acceptor activities of bovine neurophysins I and II for the enzyme protein carboxymethylase (EC 2.1.1.24) were found to be similar and as high as for other previously identified, biologically active protein substrates. Effects on the rate of methylation of these neurophysins were investigated with the posterior pituitary hormone ligands, oxytocin and vasopressin, and the hormone-related tripeptide ligand, methionyl-tyrosyl-phenylalaninamide. An increase in the rate of neurophysin II methylation was observed with both oxytocin and tripeptide. This ligand-induced response did not occur with either native neurophysin I or disulfide-scrambled neurophysin II.
Diliberto
E J
EJ
Laboratory of Clinical Science National Institute of Mental Health, Bethesda, Maryland 20014, USA.
Axelrod
J
J
Chaiken
I M
IM
D000818:Animals; D002417:Cattle; D007700:Kinetics; D008024:Ligands; D008745:Methylation / Q000187:drug effects; D009481:Neurophysins / Q000737:chemistry / Q000378:metabolism*; D009842:Oligopeptides / Q000378:metabolism / Q000494:pharmacology; D010121:Oxytocin / Q000378:metabolism / Q000494:pharmacology; D011489:Protein Denaturation; D011497:Protein O-Methyltransferase / Q000378:metabolism*; D013379:Substrate Specificity; D014667:Vasopressins / Q000378:metabolism / Q000494:pharmacology
D008024:Ligands; D009481:Neurophysins; D009842:Oligopeptides; C495291:methionyl-tyrosyl-phenylalaninamide; D014667:Vasopressins; D010121:Oxytocin; D011497:Protein O-Methyltransferase