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Literature summary for 3.4.24.7 extracted from
- pH dependence of the enzymatic processing of collagen I by MMP-1 (fibroblast collagenase), MMP-2 (gelatinase A), and MMP-14 ectodomain (2010), J. Biol. Inorg. Chem., 15, 1219-1232.
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.00025 | - |
collagen I alpha-2 chain | pH not specified in the publication, 37°C, MMP-1: 1-protonated | Homo sapiens | |
| 0.00086 | - |
collagen I alpha-1 chain | pH not specified in the publication, 37°C, MMP-1: 1-protonated | Homo sapiens | |
| 0.0011 | - |
collagen I alpha-1 chain | pH not specified in the publication, 37°C, MMP-1: 1-protonated | Homo sapiens | |
| 0.0024 | - |
collagen I alpha-2 chain | pH not specified in the publication, 37°C, MMP-1: 2-protonated | Homo sapiens | |
| 0.0028 | - |
collagen I alpha-2 chain | pH not specified in the publication, 37°C, MMP-1: 1-protonated | Homo sapiens | |
| 0.004 | - |
collagen I alpha-2 chain | pH not specified in the publication, 37°C, MMP-1: 2-protonated | Homo sapiens | |
| 0.0075 | - |
collagen I alpha-1 chain | pH not specified in the publication, 37°C, MMP-1: 0-protonated | Homo sapiens | |
| 0.01 | - |
collagen I alpha-2 chain | pH not specified in the publication, 37°C, MMP-1: 0-protonated | Homo sapiens | |
| 0.016 | - |
collagen I alpha-1 chain | pH not specified in the publication, 37°C, MMP-1: 2-protonated | Homo sapiens | |
| 0.045 | - |
collagen I alpha-1 chain | pH not specified in the publication, 37°C, MMP-1: 0-protonated | Homo sapiens | |
| 0.12 | - |
collagen I alpha-1 chain | pH not specified in the publication, 37°C, MMP-1: 3-protonated | Homo sapiens | |
| 0.14 | - |
collagen I alpha-2 chain | pH not specified in the publication, 37°C, MMP-1: 3-protonated | Homo sapiens | |
| 0.17 | - |
collagen I alpha-1 chain | pH not specified in the publication, 37°C, MMP-1: 2-protonated | Homo sapiens | |
| 0.46 | - |
collagen I alpha-2 chain | pH not specified in the publication, 37°C, MMP-1: 3-protonated | Homo sapiens | |
| 0.53 | - |
collagen I alpha-2 chain | pH not specified in the publication, 37°C, MMP-1: 0-protonated | Homo sapiens | |
| 0.74 | - |
collagen I alpha-1 chain | pH not specified in the publication, 37°C, MMP-1: 3-protonated | Homo sapiens |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| (7-methoxycoumarin-4-yl)acetyl-Pro-cyclohexylalanine-Gly-Nve-His-Ala-(N-3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-NH2 + H2O | degradation of synthetic substrate is pH-independent | Homo sapiens | ? | - |
? |  |
| collagen I alpha-1 chain + H2O | MMP-14 ectodomain preferentially cleaves the alpha-1 chain | Homo sapiens | ? | - |
? | |
| collagen I alpha-1 chain + H2O | the overall enzymatic activity is higher on the alpha-2 chain for MMP-1 and MMP-2 | Homo sapiens | ? | - |
? | |
| collagen I alpha-2 chain + H2O | MMP-14 ectodomain preferentially cleaves the alpha-1 chain | Homo sapiens | ? | - |
? | |
| collagen I alpha-2 chain + H2O | the overall enzymatic activity is higher on the alpha-2 chain for MMP-1 and MMP-2 | Homo sapiens | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| ect-MMP-14 | ectodomain | Homo sapiens |
| MMP-1 | - |
Homo sapiens |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
assay at | Homo sapiens |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.014 | - |
collagen I alpha-2 chain | pH not specified in the publication, 37°C, MMP-1: 2-protonated | Homo sapiens | |
| 0.089 | - |
collagen I alpha-2 chain | pH not specified in the publication, 37°C, MMP-1: 1-protonated | Homo sapiens | |
| 0.21 | - |
collagen I alpha-1 chain | pH not specified in the publication, 37°C, MMP-1: 0-protonated | Homo sapiens | |
| 0.3 | - |
collagen I alpha-1 chain | pH not specified in the publication, 37°C, MMP-1: 1-protonated | Homo sapiens | |
| 0.43 | - |
collagen I alpha-1 chain | pH not specified in the publication, 37°C, MMP-1: 2-protonated | Homo sapiens | |
| 0.54 | - |
collagen I alpha-2 chain | pH not specified in the publication, 37°C, MMP-1: 3-protonated | Homo sapiens | |
| 0.65 | - |
collagen I alpha-1 chain | pH not specified in the publication, 37°C, MMP-1: 3-protonated | Homo sapiens | |
| 0.66 | - |
collagen I alpha-1 chain | pH not specified in the publication, 37°C, MMP-1: 1-protonated | Homo sapiens | |
| 0.79 | - |
collagen I alpha-2 chain | pH not specified in the publication, 37°C, MMP-1: 2-protonated | Homo sapiens | |
| 1.83 | - |
collagen I alpha-1 chain | pH not specified in the publication, 37°C, MMP-1: 2-protonated | Homo sapiens | |
| 4.09 | - |
collagen I alpha-2 chain | pH not specified in the publication, 37°C, MMP-1: 3-protonated | Homo sapiens | |
| 4.56 | - |
collagen I alpha-1 chain | pH not specified in the publication, 37°C, MMP-1: 0-protonated | Homo sapiens | |
| 5.44 | - |
collagen I alpha-2 chain | pH not specified in the publication, 37°C, MMP-1: 1-protonated | Homo sapiens | |
| 10.41 | - |
collagen I alpha-1 chain | pH not specified in the publication, 37°C, MMP-1: 3-protonated | Homo sapiens | |
| 16.9 | - |
collagen I alpha-2 chain | pH not specified in the publication, 37°C, MMP-1: 0-protonated | Homo sapiens | |
| 58.61 | - |
collagen I alpha-2 chain | pH not specified in the publication, 37°C, MMP-1: 0-protonated | Homo sapiens |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 6 | 9.2 | degradation of collagen I: at pH 7.5 a 10fold higher activity is observed toward the alpha-2 chain, whereas a very similar value for the two chains is detected at pH 7.0. At pH lower 7.0 the overall enzymatic activity toward the alpha-1 chain increases, whereas the processing of the alpha-2 chain remains essentially constant between pH 7.3 and 6.0 | Homo sapiens |
| 6 | 9.2 | degradation of collagen I: over the whole pH range investigated the proteolytic activity on the alpha2 chains is higher than for the alpha1 chain. Difference is large at alkaline pH (40fold at pH 9.2) and it decreases as the pH decreases toward the physiological value where the enzymatic processing of the alpha2 chain is only 4times higher than for the alpha1 chain. Difference remains essentially unchanged down to pH 6.3 | Homo sapiens |
| 6 | 9.2 | degradation of synthetic substrate is pH-independent | Homo sapiens |
| 6 | 9.2 | degradation of synthetic substrate: overall enzymatic activity of ect-MMP-14 displays a pH dependence characterized by maximum efficiency at pH 7.0, which decreases upon both pH increase and pH decrease | Homo sapiens |
kcat/KM [mM/s]
| kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.88 | - |
collagen I alpha-1 chain | pH not specified in the publication, 37°C, MMP-1: 3-protonated | Homo sapiens | |
| 1.2 | - |
collagen I alpha-2 chain | pH not specified in the publication, 37°C, MMP-1: 3-protonated | Homo sapiens | |
| 2.5 | - |
collagen I alpha-1 chain | pH not specified in the publication, 37°C, MMP-1: 2-protonated | Homo sapiens | |
| 3.5 | - |
collagen I alpha-2 chain | pH not specified in the publication, 37°C, MMP-1: 2-protonated | Homo sapiens | |
| 28 | - |
collagen I alpha-1 chain | pH not specified in the publication, 37°C, MMP-1: 0-protonated | Homo sapiens | |
| 30 | - |
collagen I alpha-2 chain | pH not specified in the publication, 37°C, MMP-1: 3-protonated | Homo sapiens | |
| 88 | - |
collagen I alpha-1 chain | pH not specified in the publication, 37°C, MMP-1: 3-protonated | Homo sapiens | |
| 100 | - |
collagen I alpha-1 chain | pH not specified in the publication, 37°C, MMP-1: 0-protonated | Homo sapiens | |
| 110 | - |
collagen I alpha-2 chain | pH not specified in the publication, 37°C, MMP-1: 0-protonated | Homo sapiens | |
| 120 | - |
collagen I alpha-1 chain | pH not specified in the publication, 37°C, MMP-1: 2-protonated | Homo sapiens | |
| 330 | - |
collagen I alpha-2 chain | pH not specified in the publication, 37°C, MMP-1: 2-protonated | Homo sapiens | |
| 350 | - |
collagen I alpha-2 chain | pH not specified in the publication, 37°C, MMP-1: 1-protonated | Homo sapiens | |
| 360 | - |
collagen I alpha-1 chain | pH not specified in the publication, 37°C, MMP-1: 1-protonated | Homo sapiens | |
| 630 | - |
collagen I alpha-1 chain | pH not specified in the publication, 37°C, MMP-1: 1-protonated | Homo sapiens | |
| 1600 | - |
collagen I alpha-2 chain | pH not specified in the publication, 37°C, MMP-1: 0-protonated | Homo sapiens | |
| 1900 | - |
collagen I alpha-2 chain | pH not specified in the publication, 37°C, MMP-1: 1-protonated | Homo sapiens |
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