Dynorphin-degrading cysteine protease is highly specific for paired arginine residues.
The cleavage of dynorphin and three analogs containing paired basic residues by several proteases was investigated. The cysteine protease of neuroblastoma cells cleaved only the bond between Arg-Arg residues. Submandibular arginyl-endopeptidase, however, cleaved bonds between both Arg-Arg and Arg-Lys residues, and pancreatic trypsin at the carboxyl sides of both arginine and lysine residues. This shows that the cysteine protease is highly specific for paired arginine residues.
Department of Biochemistry, Faculty of Pharmaceutical Sciences, Hokkaido University, Sapporo, Japan.
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Watanabe
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Ishii
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Yokosawa
D000595:Amino Acid Sequence; D000818:Animals; D003546:Cysteine Endopeptidases / Q000378:metabolism*; D004399:Dynorphins / Q000031:analogs & derivatives / Q000378:metabolism*; D007700:Kinetics; D051379:Mice; D008969:Molecular Sequence Data; D012697:Serine Endopeptidases / Q000302:isolation & purification / Q000378:metabolism*; D013363:Submandibular Gland / Q000201:enzymology; D013379:Substrate Specificity
D004399:Dynorphins; D012697:Serine Endopeptidases; C060325:arginine endopeptidase; D003546:Cysteine Endopeptidases