EC 22.214.171.124 - Scytalidopepsin B
IntEnz Enzyme Nomenclature
Ganoderma lucidum carboxyl proteinase
Scytalidium lignicolum aspartic proteinase B
Scytalidium aspartic proteinase B
- Hydrolysis of proteins with broad specificity, cleaving Phe24┼Phe, but not Leu15-Tyr and Phe25-Tyr in the B chain of insulin.
A second endopeptidase from Scytalidium lignicolum (see scytalidopepsin A) that is insensitive to pepstatin and methyl 2-diazoacetamidohexanoate. 1,2-Epoxy-3-(p-nitrophenoxy)propane reacts with Glu53, which replaces one of the aspartic residues at the active centre. One of the smallest aspartic endopeptidases active as the monomer, with Mr 22,000. Similarly inhibitor-resistant endopeptidases are found in the basidiomycetes Lentinus edodes  and Ganoderma lucidum , and in Polyporus tulipiferae , a second endopeptidase distinct from polyporopepsin, but these are of typical aspartic endopeptidase size, Mr about 36,000. Type example of peptidase family G1.
Links to other databases
Streptomyces pepsin inhibitor-insensitive carboxyl proteinase from Lentinus edodes.Agric. Biol. Chem. 45: 1937-1943 (1981).
Complete amino acid sequence of Scytalidium lignicolum acid protease B.J. Biochem. (Tokyo) 95: 465-473 (1984).
Streptomyces pepsin inhibitor-insensitive carboxyl proteinase from Ganoderma lucidum.Agric. Biol. Chem. 48: 1029-1035 (1984). [PMID: 6370989]
Purification and characterization of a pepstatin-insensitive carboxyl proteinase from Polyporus tulipiferae (Irpex lacteus).Agric. Biol. Chem. 49: 2393-2397 (1985). [PMID: 6370989]
Isolation and amino acid sequence of a peptide containing an epoxide-reactive residue from the thermolysin-digest of Scytalidium lignicolum acid protease B.J. Biochem. (Tokyo) 99: 1537-1539 (1986). [PMID: 3519605]
[EC 126.96.36.199 created 1992]