A putative processing enzyme from Aplysia that cleaves dynorphin A at the single arginine residue.
A peptidase activity cleaving at single arginine residues has been detected in extracts of the atrial gland of Aplysia Californica. The enzyme assay consisted of incubation of enzyme with the mammalian opioid peptide dynorphin A and detection by specific radioimmunoassay of dynorphin (1-8), a single arginine cleavage product. The peptidase activity was characterized following chromatography on DEAE-cellulose. Activity was abolished by a thiol-directed inhibitor and chelators and activated by dithiothreitol and cobalt chloride. The pH optimum was 6.2 in phosphate buffer. Analysis of the products of two substrates suggested that cleavage was occurring on the amino side of the arginine residue.
D000107:Acetylation; D000818:Animals; D001048:Aplysia / Q000201:enzymology*; D001120:Arginine; D004399:Dynorphins; D004723:Endorphins / Q000378:metabolism*; D010446:Peptide Fragments / Q000378:metabolism*; D010447:Peptide Hydrolases / Q000378:metabolism*; D011480:Protease Inhibitors / Q000494:pharmacology; D013379:Substrate Specificity
D004723:Endorphins; D010446:Peptide Fragments; D011480:Protease Inhibitors; D004399:Dynorphins; C026770:dynorphin (1-8); D001120:Arginine; D010447:Peptide Hydrolases