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Literature summary for 3.4.21.1 extracted from

  • Case, A.; Huskey, W.P.; Stein, R.L.
    Enzymatic reaction of silent substrates: kinetic theory and application to the serine protease chymotrypsin (2003), Biochemistry, 42, 4727-4732.
    View publication on PubMed
Search for more literature for 3.4.21.1

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.4
-
 N-succinyl-Ala-Phe-Ala 30°C, pH 8.0, determined by competition with N-succinyl-Ala-Phe-p-nitroanilide Bos taurus
0.48
-
 N-succinyl-Ala-Phe-Ala 30°C, pH 8.0, HPLC-based assay Bos taurus
2.5
-
 N-succinyl-Ala-Phe-p-nitroanilide 30°C, pH 8.0 Bos taurus

Organism

Organism UniProt Comment Textmining
Bos taurus
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
N-succinyl-Ala-Phe-Ala + H2O
-
 Bos taurus N-succinyl-Ala-Phe + alanine
-
 ?
N-succinyl-Ala-Phe-p-nitroanilide + H2O
-
 Bos taurus N-succinyl-Ala-Phe + p-nitroaniline
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.65
-
 N-succinyl-Ala-Phe-p-nitroanilide 30°C, pH 8.0 Bos taurus
0.9
-
 N-succinyl-Ala-Phe-Ala 30°C, pH 8.0, determined by competition with N-succinyl-Ala-Phe-p-nitroanilide Bos taurus
1.2
-
 N-succinyl-Ala-Phe-Ala 30°C, pH 8.0, HPLC-based assay Bos taurus