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Literature summary for 3.4.24.23 extracted from

  • Muta, Y.; Oneda, H.; Inouye, K.
    Anomalous pH-dependence of the activity of human matrilysin (matrix metalloproteinase-7) as revealed by nitration and amination of its tyrosine residues (2005), Biochem. J., 386, 263-270.
    View publication on PubMedView publication on EuropePMC
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KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information Km-value decreases from 2.57 mg/ml to 2.29 mg/ml upon nitration of 4-5 Tyr residues of enzyme, pH 7.5, 25°C Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Azocoll + H2O
-
 Homo sapiens ?
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
-
 additional information kcat-value decreases from 337 mg/ml x M x s to 305 mg/ml x M x s upon nitration of 4-5 Tyr residues of enzyme, pH 7.5, 25°C Homo sapiens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
additional information
-
 upon nitration of 4 or 5 Tyr residues, activity at pH 7 decreases significantly, while that at pH 7-10 is unchanged, leading to anomalous pH-dependence with an additional third pKa-value at 6.2-6.4 Homo sapiens