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Literature summary extracted from

  • Bauer, C.A.
    Active centers of alpha-chymotrypsin and of Streptomyces griseus proteases 1 and 3. S2-P2 enzyme-substrate interactions (1980), Eur. J. Biochem., 105, 565-570.
    View publication on PubMed

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.4.21.80 additional information
-
 additional information
-
 Streptomyces griseus
3.4.21.80 0.45
-
 Acetyl-Pro-Ala-Leu-Phe-NH2
-
 Streptomyces griseus
3.4.21.80 0.54
-
 Acetyl-Pro-Ala-Pro-Phe-NH2
-
 Streptomyces griseus
3.4.21.81 additional information
-
 additional information
-
 Streptomyces griseus
3.4.21.81 1.4
-
 Acetyl-Pro-Ala-Leu-Phe-NH2
-
 Streptomyces griseus
3.4.21.81 2.4
-
 Acetyl-Pro-Ala-Pro-Phe-NH2
-
 Streptomyces griseus

Organism

EC Number Organism UniProt Comment Textmining
3.4.21.80 Streptomyces griseus
-
-
-
3.4.21.81 Streptomyces griseus
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.21.80 3 acetyl-Pro-Ala-Phe-Phe-NH2 + H2O hydrolyzed at the Ala-Phe, the Phe-Phe and the Phe-NH2 bonds Streptomyces griseus acetyl-Pro-Ala-Phe-Phe + NH3 + acetyl-Pro-Ala + Phe-Phe-NH2 + acetyl-Pro-Ala-Phe + Phe-NH2
-
 ?
3.4.21.80 Acetyl-Pro-Ala-Ala-Phe-NH2 + H2O
-
 Streptomyces griseus ?
-
 ?
3.4.21.80 Acetyl-Pro-Ala-Gly-Phe-NH2 + H2O split at amide bond as well as at the Ala-Gly bond Streptomyces griseus ?
-
 ?
3.4.21.80 Acetyl-Pro-Ala-Leu-Phe-NH2 + H2O hydrolyzed at the amide bond only Streptomyces griseus Acetyl-Pro-Ala-Leu-Phe-OH + NH3
-
 ?
3.4.21.80 Acetyl-Pro-Ala-Pro-Phe-NH2 + H2O hydrolyzed at the amide bond only Streptomyces griseus Acetyl-Pro-Ala-Pro-Phe-OH + NH3
-
 ?
3.4.21.80 Peptide + H2O interacts favorably with peptides with hydrophobic non-aromatic, P2 amino acid residues, leucine being optimal Streptomyces griseus Hydrolyzed peptide + H2O
-
 ?
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-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 additional information interacts favorably with peptides with hydrophobic non-aromatic, P2 amino acid residues, leucine being optimal Streptomyces griseus ?
-
 ?

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.4.21.81 37
-
 assay at Streptomyces griseus

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.4.21.80 additional information
-
 additional information
-
 Streptomyces griseus
3.4.21.80 5.1
-
 Acetyl-Pro-Ala-Leu-Phe-NH2
-
 Streptomyces griseus
3.4.21.80 5.8
-
 Acetyl-Pro-Ala-Pro-Phe-NH2
-
 Streptomyces griseus
3.4.21.81 additional information
-
 additional information
-
 Streptomyces griseus
3.4.21.81 6.7
-
 Acetyl-Pro-Ala-Pro-Phe-NH2
-
 Streptomyces griseus
3.4.21.81 7.1
-
 Acetyl-Pro-Ala-Leu-Phe-NH2
-
 Streptomyces griseus