Inhibitors | Comment | Organism | Structure |
---|---|---|---|
batimastat | - |
Homo sapiens |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.00025 | - |
collagen type I alpha-2 chain | 1-protonated enzyme, 50 mM Tris-HCl, 0.1 M NaCl, 10 mM CaCl2 plus 0.05% Brij 35,at pH 7.3 and 37°C | Homo sapiens | |
0.0003 | - |
collagen I alpha-1 chain | pH not specified in the publication, 37°C, MMP-1: 1-protonated | Homo sapiens | |
0.00065 | - |
collagen I alpha-2 chain | pH not specified in the publication, 37°C, MMP-1: 3-protonated | Homo sapiens | |
0.00077 | - |
collagen I alpha-1 chain | pH not specified in the publication, 37°C, MMP-1: 2-protonated | Homo sapiens | |
0.00086 | - |
collagen type I alpha-1 chain | 1-protonated enzyme, 50 mM Tris-HCl, 0.1 M NaCl, 10 mM CaCl2 plus 0.05% Brij 35,at pH 7.3 and 37°C | Homo sapiens | |
0.0027 | - |
collagen I alpha-1 chain | pH not specified in the publication, 37°C, MMP-1: 0-protonated | Homo sapiens | |
0.0031 | - |
collagen I alpha-2 chain | pH not specified in the publication, 37°C, MMP-1: 0-protonated | Homo sapiens | |
0.004 | - |
collagen type I alpha-2 chain | 2-protonated enzyme, 50 mM Tris-HCl, 0.1 M NaCl, 10 mM CaCl2 plus 0.05% Brij 35,at pH 7.3 and 37°C | Homo sapiens | |
0.0079 | - |
collagen I alpha-2 chain | pH not specified in the publication, 37°C, MMP-1: 1-protonated | Homo sapiens | |
0.045 | - |
collagen type I alpha-1 chain | 0-protonated enzyme, 50 mM Tris-HCl, 0.1 M NaCl, 10 mM CaCl2 plus 0.05% Brij 35,at pH 7.3 and 37°C | Homo sapiens | |
0.12 | - |
collagen I alpha-2 chain | pH not specified in the publication, 37°C, MMP-1: 2-protonated | Homo sapiens | |
0.12 | - |
collagen type I alpha-1 chain | 3-protonated enzyme, 50 mM Tris-HCl, 0.1 M NaCl, 10 mM CaCl2 plus 0.05% Brij 35,at pH 7.3 and 37°C | Homo sapiens | |
0.14 | - |
collagen type I alpha-2 chain | 3-protonated enzyme, 50 mM Tris-HCl, 0.1 M NaCl, 10 mM CaCl2 plus 0.05% Brij 35,at pH 7.3 and 37°C | Homo sapiens | |
0.17 | - |
collagen type I alpha-1 chain | 2-protonated enzyme, 50 mM Tris-HCl, 0.1 M NaCl, 10 mM CaCl2 plus 0.05% Brij 35,at pH 7.3 and 37°C | Homo sapiens | |
0.32 | - |
collagen I alpha-1 chain | pH not specified in the publication, 37°C, MMP-1: 3-protonated | Homo sapiens | |
0.53 | - |
collagen type I alpha-2 chain | 0-protonated enzyme, 50 mM Tris-HCl, 0.1 M NaCl, 10 mM CaCl2 plus 0.05% Brij 35,at pH 7.3 and 37°C | Homo sapiens |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
membrane | - |
Homo sapiens | 16020 | - |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
(7-methoxycoumarin-4-yl)acetyl-Pro-cyclohexylalanine-Gly-norvaline-His-Ala-(N-3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-NH2 + H2O | degradation of synthetic substrate is pH-independent | Homo sapiens | ? | - |
? | |
(7-methoxycoumarin-4-yl)acetyl-Pro-Leu-Ala-Cys(p-OMeBz)-Trp-Ala-Arg(N-3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-NH2 + H2O | - |
Homo sapiens | ? | - |
? | |
collagen I alpha-1 chain + H2O | overall enzymatic activity is higher on the alpha-2 chain for both MMP-1 and MMP-2. In MMP-2 a marked difference for substrate affinity (higher for the alpha-1 chain) is overwhelmed by an even more marked propensity to cleave the alpha-2 chain | Homo sapiens | ? | - |
? | |
collagen I alpha-2 chain + H2O | overall enzymatic activity is higher on the alpha-2 chain for both MMP-1 and MMP-2. In MMP-2 a marked difference for substrate affinity (higher for the alpha-1 chain) is overwhelmed by an even more marked propensity to cleave the alpha-2 chain | Homo sapiens | ? | - |
? | |
collagen type I alpha-1 chain + H2O | the MMP-14 ectodomain preferentially cleaves the alpha-1 chain of collagen type I | Homo sapiens | ? | - |
? | |
collagen type I alpha-2 chain + H2O | - |
Homo sapiens | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
gelatinase A | - |
Homo sapiens |
matrix metalloproteinase 14 | - |
Homo sapiens |
MMP-14 | - |
Homo sapiens |
MMP-2 | - |
Homo sapiens |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Homo sapiens |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.0089 | - |
collagen type I alpha-2 chain | 1-protonated enzyme, 50 mM Tris-HCl, 0.1 M NaCl, 10 mM CaCl2 plus 0.05% Brij 35,at pH 7.3 and 37°C | Homo sapiens | |
0.014 | - |
collagen type I alpha-2 chain | 2-protonated enzyme, 50 mM Tris-HCl, 0.1 M NaCl, 10 mM CaCl2 plus 0.05% Brij 35,at pH 7.3 and 37°C | Homo sapiens | |
0.019 | - |
collagen I alpha-1 chain | pH not specified in the publication, 37°C, MMP-1: 1-protonated | Homo sapiens | |
0.3 | - |
collagen type I alpha-1 chain | 1-protonated enzyme, 50 mM Tris-HCl, 0.1 M NaCl, 10 mM CaCl2 plus 0.05% Brij 35,at pH 7.3 and 37°C | Homo sapiens | |
0.43 | - |
collagen type I alpha-1 chain | 2-protonated enzyme, 50 mM Tris-HCl, 0.1 M NaCl, 10 mM CaCl2 plus 0.05% Brij 35,at pH 7.3 and 37°C | Homo sapiens | |
0.47 | - |
collagen I alpha-1 chain | pH not specified in the publication, 37°C, MMP-1: 0-protonated | Homo sapiens | |
0.68 | - |
collagen I alpha-1 chain | pH not specified in the publication, 37°C, MMP-1: 2-protonated | Homo sapiens | |
1.1 | - |
collagen I alpha-1 chain | pH not specified in the publication, 37°C, MMP-1: 3-protonated | Homo sapiens | |
1.52 | - |
collagen I alpha-2 chain | pH not specified in the publication, 37°C, MMP-1: 3-protonated | Homo sapiens | |
4.09 | - |
collagen type I alpha-2 chain | 4-protonated enzyme, 50 mM Tris-HCl, 0.1 M NaCl, 10 mM CaCl2 plus 0.05% Brij 35,at pH 7.3 and 37°C | Homo sapiens | |
4.56 | - |
collagen type I alpha-1 chain | 0-protonated enzyme, 50 mM Tris-HCl, 0.1 M NaCl, 10 mM CaCl2 plus 0.05% Brij 35,at pH 7.3 and 37°C | Homo sapiens | |
5.79 | - |
collagen I alpha-2 chain | pH not specified in the publication, 37°C, MMP-1: 1-protonated | Homo sapiens | |
9.89 | - |
collagen I alpha-2 chain | pH not specified in the publication, 37°C, MMP-1: 0-protonated | Homo sapiens | |
10.41 | - |
collagen type I alpha-1 chain | 4-protonated enzyme, 50 mM Tris-HCl, 0.1 M NaCl, 10 mM CaCl2 plus 0.05% Brij 35,at pH 7.3 and 37°C | Homo sapiens | |
58.61 | - |
collagen type I alpha-2 chain | 0-protonated enzyme, 50 mM Tris-HCl, 0.1 M NaCl, 10 mM CaCl2 plus 0.05% Brij 35,at pH 7.3 and 37°C | Homo sapiens | |
255.6 | - |
collagen I alpha-2 chain | pH not specified in the publication, 37°C, MMP-1: 2-protonated | Homo sapiens |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
6 | 9.2 | degradation of collagen I: over the whole pH range investigated the enzymatic activity toward the alpha-2 chain is significantly higher than that toward the alpha-1 chain. Difference is maximal at alkaline pH (being about 20fold at pH 9.2) and it decreases at neutral pH, such that at pH 7.3 the enzymatic processing of the alpha-2 chain is only about 5fold higher than for the alpha-1 chain | Homo sapiens |
kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
2.5 | - |
collagen type I alpha-1 chain | 2-protonated enzyme, 50 mM Tris-HCl, 0.1 M NaCl, 10 mM CaCl2 plus 0.05% Brij 35,at pH 7.3 and 37°C | Homo sapiens | |
3.4 | - |
collagen I alpha-1 chain | pH not specified in the publication, 37°C, MMP-1: 3-protonated | Homo sapiens | |
3.5 | - |
collagen type I alpha-2 chain | 2-protonated enzyme, 50 mM Tris-HCl, 0.1 M NaCl, 10 mM CaCl2 plus 0.05% Brij 35,at pH 7.3 and 37°C | Homo sapiens | |
30 | - |
collagen type I alpha-2 chain | 4-protonated enzyme, 50 mM Tris-HCl, 0.1 M NaCl, 10 mM CaCl2 plus 0.05% Brij 35,at pH 7.3 and 37°C | Homo sapiens | |
63 | - |
collagen I alpha-1 chain | pH not specified in the publication, 37°C, MMP-1: 1-protonated | Homo sapiens | |
88 | - |
collagen type I alpha-1 chain | 4-protonated enzyme, 50 mM Tris-HCl, 0.1 M NaCl, 10 mM CaCl2 plus 0.05% Brij 35,at pH 7.3 and 37°C | Homo sapiens | |
100 | - |
collagen type I alpha-1 chain | O-protonated enzyme, 50 mM Tris-HCl, 0.1 M NaCl, 10 mM CaCl2 plus 0.05% Brij 35,at pH 7.3 and 37°C | Homo sapiens | |
110 | - |
collagen type I alpha-2 chain | O-protonated enzyme, 50 mM Tris-HCl, 0.1 M NaCl, 10 mM CaCl2 plus 0.05% Brij 35,at pH 7.3 and 37°C | Homo sapiens | |
170 | - |
collagen I alpha-1 chain | pH not specified in the publication, 37°C, MMP-1: 0-protonated | Homo sapiens | |
350 | - |
collagen type I alpha-2 chain | 1-protonated enzyme, 50 mM Tris-HCl, 0.1 M NaCl, 10 mM CaCl2 plus 0.05% Brij 35,at pH 7.3 and 37°C | Homo sapiens | |
360 | - |
collagen type I alpha-1 chain | 1-protonated enzyme, 50 mM Tris-HCl, 0.1 M NaCl, 10 mM CaCl2 plus 0.05% Brij 35,at pH 7.3 and 37°C | Homo sapiens | |
730 | - |
collagen I alpha-2 chain | pH not specified in the publication, 37°C, MMP-1: 1-protonated | Homo sapiens | |
880 | - |
collagen I alpha-1 chain | pH not specified in the publication, 37°C, MMP-1: 2-protonated | Homo sapiens | |
2100 | - |
collagen I alpha-2 chain | pH not specified in the publication, 37°C, MMP-1: 2-protonated | Homo sapiens | |
2300 | - |
collagen I alpha-2 chain | pH not specified in the publication, 37°C, MMP-1: 3-protonated | Homo sapiens | |
3200 | - |
collagen I alpha-2 chain | pH not specified in the publication, 37°C, MMP-1: 0-protonated | Homo sapiens |