EC Number |
Substrates |
Organism |
Products |
Reversibility |
---|
3.4.23.22 | Abz-Thr-Ile-Nle-4-nitro-Phe-Gln-Arg-NH2 + H2O |
- |
Cryphonectria parasitica |
Abz-Thr-Ile-Nle + 4-nitro-Phe-Gln-Arg-NH2 |
- |
? |
3.4.23.22 | casein + H2O |
splits 29.0% of the peptide bonds |
Cryphonectria parasitica |
? |
- |
? |
3.4.23.22 | FVNQHLCGSHLVEALYLVCGERGFFYTPKA + H2O |
i.e. oxidized insulin B chain, cleavage site specificity |
Cryphonectria parasitica |
FVN + Gln + HLCGSHL + VEALY + LVCGERGF + FYTPKA |
- |
? |
3.4.23.22 | kappa-casein + H2O |
reaction contributes to milk-clotting activity, cleavage site specificity for Ser104-Phe105 |
Cryphonectria parasitica |
? |
- |
? |
3.4.23.22 | more |
clots milk, not: benzyloxycarbonyl-L-Glu-L-Tyr |
Cryphonectria parasitica |
? |
- |
? |
3.4.23.22 | more |
the enzyme prefers protein substrates with hydrophobic amino acid residues at P1 and P1' positions |
Cryphonectria parasitica |
? |
- |
? |
3.4.23.22 | Oxidized B-chain of insulin + H2O |
the Phe24-Phe25 bond is hydrolyzed at a maximal rate followed by hydrolysis of the Tyr16-Leu17 and Gln4-His5 bonds. The Leu11-Val12 and Asn3-Gln4 bonds are hydrolyzed at slower rates. The Leu11-Val12 bond appears to be considerably more resistant to hydrolysis in the peptide 5-16 than in the intact oxidized B-chain. The Leu15-Tyr16 bond is very slowly hydrolyzed in the peptide 5-16, no hydrolysis in the intact oxidized B-chain. Phe25 is slowly hydrolyzed from the peptide 25-30 and the bond involving Gly20-Glu21 is slowly hydrolyzed in peptide 12-24 and/or peptide 17-24 |
Cryphonectria parasitica |
? |
- |
? |
3.4.23.22 | Pepsin + H2O |
splits 8.0% of the peptide bonds |
Cryphonectria parasitica |
? |
- |
? |
3.4.23.22 | Rennin + H2O |
splits 10.2% of the peptide bonds |
Cryphonectria parasitica |
? |
- |
? |