C-terminal amidation of neuropeptides. Gly-Lys-Arg extension an efficient precursor of C-terminal amide.
Biosynthesis of the C-terminal carboxamide group of peptide hormones was studied using comparatively pGlu-His-Pro-Gly and Glu-His-Pro-Gly-Lys-Arg as putative precursors of the tripeptide, thyroliberin (TRH). Rat hypothalamus granules were found to contain an amide group forming activity which converts both peptide substrates into TRH. Comparison of the rate of conversion of the two substrates indicated that the C-terminal dibasic extension favored a 10-fold increase in the production of amidated peptide. It is suggested that this type of structure may be present in the putative biosynthetic precursor of TRH and that it may provide a better substrate for the enzyme(s) involved in C-terminal amidation.
D000818:Animals; D003594:Cytoplasmic Granules / Q000378:metabolism; D007031:Hypothalamus / Q000378:metabolism; D008297:Male; D011498:Protein Precursors / Q000378:metabolism; D011761:Pyrrolidonecarboxylic Acid / Q000031:analogs & derivatives; D051381:Rats; D011919:Rats, Inbred Strains; D013973:Thyrotropin-Releasing Hormone / Q000031:analogs & derivatives / Q000096:biosynthesis* / Q000378:metabolism
D011498:Protein Precursors; D013973:Thyrotropin-Releasing Hormone; C040476:thyrotropin-releasing hormone, Gly; C040477:thyrotropin-releasing hormone, Gly-Lys-Arg-; D011761:Pyrrolidonecarboxylic Acid