Gly and Leu17Val in the B chain of insulin
Reaction: Hydrolysis of proteins with specificity similar to that of pepsin A, but also cleaves Cys(SO3H)7Gly and Leu17Val in the B chain of insulin
Other names: Scytalidium aspartic proteinase A; Scytalidium lignicolum aspartic proteinase; Scytalidium lignicolum aspartic proteinase A-2; Scytalidium lignicolum aspartic proteinase A-I; Scytalidium lignicolum aspartic proteinase C; Scytalidium lignicolum carboxyl proteinase; Scytalidium lignicolum acid proteinase
Comments: Isolated from the imperfect fungus Scytalidium lignicolum. Not inhibited by pepstatin-Ac, methyl 2-diazoacetamidohexanoate or 1,2-epoxy-3-(p-nitrophenyl)propane. A related enzyme from the same organism, proteinase C, is also insensitive to these inhibitors and has Mr = 406,000 [3]
Links to other databases: BRENDA, EXPASY, KEGG, MEROPS, Metacyc, CAS registry number: 42613-34-3
References:
1. Oda, K. and Murao, S. Purification and some enzymatic properties of acid protease A and B of Scytalidium lignicolum ATCC 24568. Agric. Biol. Chem. 38 (1974) 2435-2444
2. Oda, K. and Murao, S. Action of Scytalidium lignicolum acid proteases on insulin B-chain. Agric. Biol. Chem. 40 (1976) 1221-1225
3. Oda, K., Torishima, H. and Murao, S. Purification and characterization of acid proteinase C of Scytalidium lignicolum ATCC 24568. Agric. Biol. Chem. 50 (1986) 651-658