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The specificity of the neuroendocrine convertase PC3 is determined by residues NH2‐ and COOH‐terminal to the cleavage site
Author(s) -
Ledgerwood Elizabeth C.,
Brennan Stephen O.,
Birch Nigel P.,
George Peter M.
Publication year - 1996
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1080/15216549600201352
Subject(s) - cleavage (geology) , dibasic acid , chemistry , residue (chemistry) , peptide , amino acid residue , amino acid , biochemistry , stereochemistry , recombinant dna , peptide sequence , biology , organic chemistry , paleontology , fracture (geology) , gene
The Kex2‐like convertase PC3 (PC1) has been implicated in the processing of a number of prohormones and proneuropeptides. In order to be able to more accurately predict substrates for PC3 its specificity was defined using recombinant proalbumins and synthetic peptide substrates. P2P1 and P4P1 dibasic sites were cleaved with similar efficiencies however there were specific restrictions on amino acids NH2‐ and COOH‐terminal to the cleavage site. His was disallowed at P2 and basic residues were forbidden at P1′. The presence of a charged residue at P2′ either completely prevented (Arg) or seriously impaired (Glu) cleavage by PC3 and the presence of a P4 Arg did not significantly increase its activity.