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Literature summary for 3.4.21.80 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
Search for more literature for 3.4.21.80

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information
-
 Streptomyces griseus
0.45
-
 Acetyl-Pro-Ala-Leu-Phe-NH2
-
 Streptomyces griseus
0.54
-
 Acetyl-Pro-Ala-Pro-Phe-NH2
-
 Streptomyces griseus

Organism

Organism UniProt Comment Textmining
Streptomyces griseus
-
-
-

Substrates and Products (Substrate)

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

Turnover Number [1/s]

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