Enzymatic arginylation of beta-melanocyte-stimulating hormone and of angiotensin II.
Porcine beta-melanocyte-stimulating hormone and angiotensin II were examined as acceptors in the reaction catalyzed by arginyl-tRNA-protein transferase. Both inhibited enzymatic transfer of [14C]arginine from tRNA to bovine albumin. Inhibition was competitive with albumin and the K-i values were, respectively, 15 and 0.8 muM. The expected arginylated compounds were isolated and characterized. Beta-melanocyte-stimulating hormone and its arginylated product had identical activities in the frog epithelium bioassay. In contrast, the biological activity of angiotensin II was diminished by enzymatic arginylation. The pressor effect of the arginylated derivative on anesthetized rats and its activity on the isolated rat uterus were, respectively, approximately 60% and 20% of those found for the unmodified peptide.
D000217:Acyltransferases / Q000378:metabolism; D000604:Amino Acyl-tRNA Synthetases / Q000378:metabolism; D000804:Angiotensin II / Q000378:metabolism*; D000818:Animals; D001120:Arginine / Q000378:metabolism*; D002417:Cattle; D004926:Escherichia coli; D007700:Kinetics; D009074:Melanocyte-Stimulating Hormones / Q000378:metabolism*; D010446:Peptide Fragments / Q000032:analysis; D012329:RNA, Bacterial / Q000378:metabolism; D012343:RNA, Transfer / Q000378:metabolism; D012710:Serum Albumin, Bovine; D013329:Structure-Activity Relationship; D013552:Swine
D010446:Peptide Fragments; D012329:RNA, Bacterial; D000804:Angiotensin II; D012710:Serum Albumin, Bovine; D009074:Melanocyte-Stimulating Hormones; D012343:RNA, Transfer; D001120:Arginine; D000217:Acyltransferases; D000604:Amino Acyl-tRNA Synthetases