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Literature summary for 3.4.21.1 extracted from

  • Bodi, A.; Kaslik, G.; Venekei, I.; Graf, L.
    Structural determinants of the half-life and cleavage site preference in the autolytic inactivation of chymotrypsin (2001), Eur. J. Biochem., 268, 6238-6246.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
F114I autolytic site Rattus norvegicus
Y146H autolytic site Rattus norvegicus
Y146H/N147S autolytic sites, altered routes of autolytic degradation Rattus norvegicus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.012
-
succinyl-Ala-Ala-Pro-Tyr-7-amido-4-methylcoumarin 37°C, pH 8.0 Rattus norvegicus
0.022
-
succinyl-Ala-Ala-Pro-Phe-7-amido-4-methylcoumarin 37°C, pH 8.0 Rattus norvegicus

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification autolytic inactivation at autolytic sites Phe114, Tyr146 and Asn147 Rattus norvegicus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
succinyl-Ala-Ala-Pro-Phe-7-amido-4-methylcoumarin + H2O
-
Rattus norvegicus succinyl-Ala-Ala-Pro-Phe + 7-amino-4-methylcoumarin
-
?
succinyl-Ala-Ala-Pro-Tyr-7-amido-4-methylcoumarin + H2O
-
Rattus norvegicus succinyl-Ala-Ala-Pro-Tyr + 7-amino-4-methylcoumarin
-
?

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
25 60 rapid inactivation above 60°C Rattus norvegicus

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
98.3
-
succinyl-Ala-Ala-Pro-Phe-7-amido-4-methylcoumarin 37°C, pH 8.0 Rattus norvegicus
105
-
succinyl-Ala-Ala-Pro-Tyr-7-amido-4-methylcoumarin 37°C, pH 8.0 Rattus norvegicus