Generation of a subunit III-like protein by autolysis of human and porcine proproteinase e in a binary complex with procarboxypeptidase A.
Tryptic treatment of human and porcine proproteinase E, procarboxypeptidase A binary complexes gave rise to active proteinase E after removal of an 11-residue N-terminal activation peptide. By contrast, upon treatment of either complex with active proteinase E, not only was the activation peptide released but also the hydrophobic dipeptide Val12-Val13 of the corresponding enzyme. No serine protease activity on specific synthetic peptide substrates could be detected. The structural homology of inactive proteinase E with subunit III of ruminant procarboxypeptidase A was strengthened by the existence of a functional homology since truncated proteinase E still possessed a weakly functional active site. Thus, subunit III-like proteins are generated by proteinase E-catalyzed limited proteolysis of proproteinase E.
Avilés
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Departament de Bioquimica í Biologia Molecular (Facultat de Ciències), Universitat Autonoma de Barcelona, Spain.
Pascual
R
R
Salva
M
M
Bonicel
J
J
Puigserver
A
A
D000595:Amino Acid Sequence; D000818:Animals; D002268:Carboxypeptidases / Q000302:isolation & purification / Q000378:metabolism*; D043422:Carboxypeptidases A; D010450:Endopeptidases / Q000302:isolation & purification / Q000378:metabolism*; D004792:Enzyme Precursors / Q000302:isolation & purification / Q000378:metabolism*; D006801:Humans; D007700:Kinetics; D046911:Macromolecular Substances; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010179:Pancreas / Q000201:enzymology; D012689:Sequence Homology, Nucleic Acid; D013552:Swine
D004792:Enzyme Precursors; D046911:Macromolecular Substances; D002268:Carboxypeptidases; D010450:Endopeptidases; C035786:pro-proteinase E; D043422:Carboxypeptidases A