EC |
3.4.23.31 |
Accepted name: |
scytalidopepsin A |
Reaction: |
Hydrolysis of proteins with specificity similar to that of pepsin A, but also cleaves Cys(SO3H)7┼Gly and Leu17┼Val in the B chain of insulin |
Other name(s): |
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, 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. |
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[EC 3.4.23.31 created 1992] |
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