EC Number   |
Substrates |
Organism |
Products |
Reversibility |
|---|
   3.4.21.81 | 3 acetyl-Pro-Ala-Phe-Phe-NH2 + H2O |
hydrolyzed at the Ala-Phe, the Phe-Phe and the Phe-NH2 bond |
Streptomyces griseus |
acetyl-Pro-Ala-Phe-Phe + NH3 + acetyl-Pro-Ala + Phe-Phe-NH2 + acetyl-Pro-Ala-Phe + Phe-NH2 |
- |
? |
| 3.4.21.81 | acetyl-Ala-Ala-Tyr-4-methylcoumarin 7-amide + H2O |
- |
Streptomyces griseus |
acetyl-Ala-Ala-Tyr + 7-amino-4-methylcoumarin |
- |
? |
| 3.4.21.81 | Acetyl-Pro-Ala-Ala-Phe-NH2 + H2O |
split at the amide bond as well as at the Ala-Ala bond |
Streptomyces griseus |
? |
- |
? |
| 3.4.21.81 | Acetyl-Pro-Ala-Gly-Phe-NH2 + H2O |
split at the amide bond as well as at the Ala-Gly bond |
Streptomyces griseus |
? |
- |
? |
| 3.4.21.81 | Acetyl-Pro-Ala-Leu-Phe-NH2 + H2O |
hydrolyzed at the amide bond only |
Streptomyces griseus |
Acetyl-Pro-Ala-Leu-Phe-OH + NH3 |
- |
? |
| 3.4.21.81 | Acetyl-Pro-Ala-Pro-Phe-NH2 + H2O |
hydrolyzed at the amide bond only |
Streptomyces griseus |
Acetyl-Pro-Ala-Pro-Phe-OH + NH3 |
- |
? |
| 3.4.21.81 | more |
interacts favorably with peptides with hydrophobic non-aromatic, P2 amino acid residues, leucine being optimal |
Streptomyces griseus |
? |
- |
? |
| 3.4.21.81 | more |
the catalytic preference of protease B for Phe, Tyr, Trp and leucyl-glycine peptide bonds under denaturing conditions enhances its utility in the site-specific proteolysis of insoluble or otherwise proteolysis-resistant polypeptide substrates |
Streptomyces griseus |
? |
- |
? |
| 3.4.21.81 | more |
member of the chymotrypsin superfamily of serine proteases |
Streptomyces griseus |
? |
- |
? |
| 3.4.21.81 | more |
upon the formation of the tetrahedral intermediate, residues Glu192A to Gly193 of SGPB move towards the alpha-carboxylate O of residue P1 of the bound species, and adjustments in the side-chain conformational angles of His57 and Ser195 of SGPB favor the progression of the catalytic mechanism of SGPB |
synthetic construct |
? |
- |
? |
