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C‐terminal amidation of neuropeptides
Author(s) -
Gomez Sophie,
di Bello Carlo,
Hung Lam Than,
Genet Roger,
Morgat Jean-Louis,
Fromageot Pierre,
Cohen Paul
Publication year - 1984
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(84)80853-4
Subject(s) - tripeptide , chemistry , peptide , amide , neuropeptide , biosynthesis , dibasic acid , substrate (aquarium) , stereochemistry , enzyme , biochemistry , peptide synthesis , oligopeptide , peptide hormone , hormone , biology , organic chemistry , ecology , receptor
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.