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Literature summary for 3.4.24.80 extracted from

  • Decaneto, E.; Suladze, S.; Rosin, C.; Havenith, M.; Lubitz, W.; Winter, R.
    Pressure and temperature effects on the activity and structure of the catalytic domain of human MT1-MMP (2015), Biophys. J., 109, 2371-2381 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.24.80

Cloned(Commentary)

Cloned (Comment) Organism
gene MMP14, recombinant expression in Escherichia coli strain BL21(DE3) Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
N-TIMP-2
-
 Homo sapiens
N-TIMP-3
-
 Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information steady-state kinetics and thermodynamics over a wide range of temperatures and pressures, stopped-flow fluorescence technique Homo sapiens
0.0006
-
 methoxycoumarin-4-acetyl-Lys-Pro-Leu-Gly-Leu-Lys(2,4-dinitrophenyl)-Ala-Arg-NH2 pH 7.0, 10°C, recombinant enzyme Homo sapiens
0.0018
-
 methoxycoumarin-4-acetyl-Lys-Pro-Leu-Gly-Leu-Lys(2,4-dinitrophenyl)-Ala-Arg-NH2 pH 7.0, 25°C, recombinant enzyme Homo sapiens
0.0021
-
 methoxycoumarin-4-acetyl-Lys-Pro-Leu-Gly-Leu-Lys(2,4-dinitrophenyl)-Ala-Arg-NH2 pH 7.0, 30°C, recombinant enzyme Homo sapiens
0.0028
-
 methoxycoumarin-4-acetyl-Lys-Pro-Leu-Gly-Leu-Lys(2,4-dinitrophenyl)-Ala-Arg-NH2 pH 7.0, 37°C, recombinant enzyme Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular matrix
-
 Homo sapiens 31012
-
membrane a transmembrane endopeptidase Homo sapiens 16020
-

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ a calcium- and zinc-dependent transmembrane endopeptidase Homo sapiens
Zn2+ a calcium- and zinc-dependent transmembrane endopeptidase Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens P50281
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
methoxycoumarin-4-acetyl-Lys-Pro-Leu-Gly-Leu-Lys(2,4-dinitrophenyl)-Ala-Arg-NH2 + H2O
-
 Homo sapiens methoxycoumarin-4-acetyl-Lys-Pro-Leu-Gly + Leu-Lys(2,4-dinitrophenyl)-Ala-Arg-NH2
-
 ?
additional information modeling of enzyme-substrate interaction Homo sapiens ?
-
 ?

Synonyms

Synonyms Comment Organism
membrane type 1-matrix metalloproteinase
-
 Homo sapiens
MMP-14
-
 Homo sapiens
MT1-MMP
-
 Homo sapiens

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
-
 Homo sapiens

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
10 55 activity range Homo sapiens

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.33
-
 methoxycoumarin-4-acetyl-Lys-Pro-Leu-Gly-Leu-Lys(2,4-dinitrophenyl)-Ala-Arg-NH2 pH 7.0, 10°C, recombinant enzyme Homo sapiens
2.1
-
 methoxycoumarin-4-acetyl-Lys-Pro-Leu-Gly-Leu-Lys(2,4-dinitrophenyl)-Ala-Arg-NH2 pH 7.0, 25°C, recombinant enzyme Homo sapiens
3.4
-
 methoxycoumarin-4-acetyl-Lys-Pro-Leu-Gly-Leu-Lys(2,4-dinitrophenyl)-Ala-Arg-NH2 pH 7.0, 30°C, recombinant enzyme Homo sapiens
6.8
-
 methoxycoumarin-4-acetyl-Lys-Pro-Leu-Gly-Leu-Lys(2,4-dinitrophenyl)-Ala-Arg-NH2 pH 7.0, 37°C, recombinant enzyme Homo sapiens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7 7.4 assay at Homo sapiens

General Information

General Information Comment Organism
additional information a small conformational change is detected at 37°C, which is responsible for the change in activity observed at the same temperature. Pressure decreases the enzymatic activity until complete inactivation occurs at 2 kbar. The inactivation is associated with changes in the rate-limiting step of the reaction caused by additional hydration of the active site upon compression and/or minor conformational changes in the active site region Homo sapiens
physiological function membrane type 1-matrix metalloproteinase (MT1-MMP or MMP-14) is involved in the degradation of extracellular matrix and tumor invasion. MT1-MMP is involved in the mediation of pericellular proteolysis of extracellular matrix components, essential for the physiological remodeling processes such as tissue repair, development, and morphogenesis. MT1-MMP is overexpressed in many cancer types and increases tumor cell growth, invasion, and metastasis by degrading extracellular matrix components and making paths through surrounding tissues Homo sapiens

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
550
-
 methoxycoumarin-4-acetyl-Lys-Pro-Leu-Gly-Leu-Lys(2,4-dinitrophenyl)-Ala-Arg-NH2 pH 7.0, 10°C, recombinant enzyme Homo sapiens
1167
-
 methoxycoumarin-4-acetyl-Lys-Pro-Leu-Gly-Leu-Lys(2,4-dinitrophenyl)-Ala-Arg-NH2 pH 7.0, 25°C, recombinant enzyme Homo sapiens
1619
-
 methoxycoumarin-4-acetyl-Lys-Pro-Leu-Gly-Leu-Lys(2,4-dinitrophenyl)-Ala-Arg-NH2 pH 7.0, 30°C, recombinant enzyme Homo sapiens
2429
-
 methoxycoumarin-4-acetyl-Lys-Pro-Leu-Gly-Leu-Lys(2,4-dinitrophenyl)-Ala-Arg-NH2 pH 7.0, 37°C, recombinant enzyme Homo sapiens