Comparison of phytolacain R, a cysteine protease from Phytolacca americana, with papain.
Nine sites of oxidized insulin B-chain were cleaved by phytolacain R, isolated from pokeweed, after 20 hr of hydrolysis. Five cleavage sites resembled those of papain. Substrate specificity of phytolacain R was similar to that of papain, preferring hydrophobic P2 residues. The activities of fibrin formation and elastin hydrolysis of phytolacain R were higher than those of papain. The amino terminal sequence of phytolacain R, although similar was not identical with that of papain.
Kaneda
M
M
Department of Chemistry, Faculty of Science, Kagoshima University, Japan.
Nagatome
S
S
Uchikoba
T
T
D000595:Amino Acid Sequence; D003546:Cysteine Endopeptidases / Q000737:chemistry / Q000378:metabolism*; D007328:Insulin / Q000378:metabolism; D007700:Kinetics; D008969:Molecular Sequence Data; D010206:Papain / Q000737:chemistry / Q000378:metabolism*; D010940:Plant Proteins / Q000737:chemistry / Q000378:metabolism*; D010944:Plants / Q000201:enzymology; D017386:Sequence Homology, Amino Acid; D013379:Substrate Specificity
D007328:Insulin; D010940:Plant Proteins; D003546:Cysteine Endopeptidases; C095519:phytolacain R; D010206:Papain