Pro-carboxypeptidase R cleaves bradykinin following activation.
Arginine carboxypeptidase (CPR) is a labile enzyme present in human serum which is unrelated to carboxypeptidase N. In this study we demonstrate that CPR exists in a precursor form in plasma and can be converted to the active form by trypsin and presumable trypsin-like enzymes. The trypsin-generated active form can not only cleave a small synthetic substrate, hippuryl-L-arginine, but can remove terminal arginine from bradykinin.
Shinohara
T
T
First Department of Surgery, Fukuoka University School of Medicine, Japan.
Sakurada
C
C
Suzuki
T
T
Takeuchi
O
O
Campbell
W
W
Ikeda
S
S
Okada
N
N
Okada
H
H
D001920:Bradykinin / Q000378:metabolism*; D004789:Enzyme Activation; D004792:Enzyme Precursors / Q000378:metabolism; D006801:Humans; D001121:Lysine Carboxypeptidase / Q000378:metabolism*; D008297:Male; D011498:Protein Precursors / Q000378:metabolism
D004792:Enzyme Precursors; D011498:Protein Precursors; D001121:Lysine Carboxypeptidase; D001920:Bradykinin