A Met-enkephalin-containing-peptide, BAM 22P, as a novel substrate for glandular kallikreins.
Homogeneous preparations of two well-characterized glandular kallikreins have been examined for their ability to hydrolyze BAM 22P, a methionine-enkephalin-containing-peptide found in the adrenal medulla. Both enzymes cleaved preferentially the Arg6-Arg7 bond in this substrate. The specificity constant (kcat/Km) for this cleavage was 86 mM-1 sec-1 for horse urinary kallikrein and 566 mM-1 sec-1 for porcine pancreatic kallikrein. These results demonstrate a previously undescribed specificity for glandular kallikreins and suggest a possible role for these widely distributed enzymes in prohormone processing.
D000818:Animals; D004744:Enkephalin, Methionine / Q000031:analogs & derivatives* / Q000378:metabolism; D006736:Horses; D006868:Hydrolysis; D007610:Kallikreins / Q000502:physiology* / Q000652:urine; D007700:Kinetics; D010179:Pancreas / Q000201:enzymology; D011498:Protein Precursors / Q000378:metabolism*; D013379:Substrate Specificity; D013552:Swine
D011498:Protein Precursors; D004744:Enkephalin, Methionine; C028837:BAM 22P; D007610:Kallikreins