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Literature summary for 3.4.24.24 extracted from
- Molecular design of a highly selective and strong protein inhibitor against matrix metalloproteinase-2 (MMP-2) (2013), J. Biol. Chem., 288, 9066-9076.
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| APP-IP-TIMP-2 | inhibition evaluation and kinetics, mechanism in concanavalin A-stimulated HT1080 fibrosarcoma cells, expression of APP-IP-TIMP-2 in HT1080 cells, overview. The ten amino acid residue sequence of APP-derived MMP-2 selective inhibitory peptide (APP-IP) is added to the N-terminus of tissue inhibitors of metalloproteinase 2, TIMP-2. The APP-IP and TIMP-2 regions of the fusion protein are designed to interact with the active site and the hemopexin-like domain of MMP-2, respectively.The reactive site of the TIMP-2 region, which has broad specificity against MMPs, is blocked by the APP-IP adduct. The recombinant APP-IP-TIMP-2 shows strong inhibitory activity toward MMP-2 whereas its inhibitory activity toward MMP-1, MMP-3, MMP-7, MMP-8, MMP-9, or MT1--MMP is six orders of magnitude or more weaker. Compared with the decapeptide APP-IP, APP-IP-TIMP-2 shows a much longer half-life in cultured tumor cells | Homo sapiens | |
| additional information | molecular design of a highly selective and strong protein inhibitor against matrix metalloproteinase-2, overview | Homo sapiens | |
| N-(R)-(2-(hydroxyaminocarbonyl)methyl)-4-methylpentanoyl-L-naphthylalanyl-L-alanine-2-aminoethyl amide | TAPI-1 | Homo sapiens |  |
| tissue inhibitors of metalloproteinase 2 | TIMP2 | Homo sapiens |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| extracellular | the enzyme is secreted | Homo sapiens | - |
- |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| Type IV collagen + H2O | Homo sapiens | degradation | ? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | P08253 | - |
- |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| proteolytic modification | the enzyme is activated by cleavage of it propeptide, activation stimulation involves concanavalin A | Homo sapiens |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| native, extracellular, inhibitor-free enzyme from glioblastoma cell line T98G cell culture medium | Homo sapiens |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| glioblastoma cell | - |
Homo sapiens | - |
| T-98G cell | - |
Homo sapiens | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| Type IV collagen + H2O | degradation | Homo sapiens | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| matrix metalloproteinase-2 | - |
Homo sapiens |
| MMP-2 | - |
Homo sapiens |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
assay at | Homo sapiens |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.5 | - |
assay at | Homo sapiens |
Ki Value [mM]
| Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.00000000068 | - |
APP-IP-TIMP-2 | pH 7.5, 37°C | Homo sapiens |
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