Activating Compound | Comment | Organism | Structure |
---|---|---|---|
additional information | the PEX domain is required for activating cleavage activity on substrate proMMP-2 on the cell surface | Homo sapiens | |
TIMP-2 | required, MT-MMP1 must form a homophilic ternary complex with TIMP-2 and pro-MMP-2 to activate MMP-2 | Homo sapiens |
Cloned (Comment) | Organism |
---|---|
recombinant expression of the truncation mutant MT1EADELTATM in Escherichia coli, expression of the PEX-domain-deleted MT1-MMP mutant | Homo sapiens |
Protein Variants | Comment | Organism |
---|---|---|
additional information | construction of truncation mutant MT1EADELTATM lacking the pro-peptide and the transmembrane and cytoplasmic domains. Mutant MT1EADELTATM shows different mobility in reducing and non-reducing PAGE compared to the wild-type enzyme, the disulfide bond in the PEX domain is correctly folded, there is no intermolecular disulfide bond formation, and the complex with TIMP-2 is also correctly formed. A PEX-domain-deleted MT1-MMP mutant is no longer able to activate proMMP-2, but retains some proteolytic activity and forms the ternery complex with proMMP-2 and TIMP-2. A MT1-MMP mutant lacking the catalytic domain is catalytically inactive and inhibits the dimerization and complex formation of the enzyme, overview | Homo sapiens |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
Rac1 | inhibits both enzyme activity and dimerization | Homo sapiens |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
cell surface | MT1-MMP forms a homophilic complex required for activity | Homo sapiens | 9986 | - |
membrane | - |
Homo sapiens | 16020 | - |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
50000 | - |
monomeric mutant MT1EADELTATM, native PAGE | Homo sapiens |
130000 | - |
dimeric mutant MT1EADELTATM, native PAGE | Homo sapiens |
600000 | - |
oligomeric mutant MT1EADELTATM, native PAGE | Homo sapiens |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
pro-MMP-2 + H2O | Homo sapiens | MT-MMP1 activates MMP-2, EC 3.4.24.24 | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | - |
- |
- |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
HT-1080 cell | - |
Homo sapiens | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
pro-MMP-2 + H2O | MT-MMP1 activates MMP-2, EC 3.4.24.24 | Homo sapiens | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
dimer | 1 * 50000, mutant MT1EADELTATM, SDS-PAGE | Homo sapiens |
monomer | 1 * 50000, mutant MT1EADELTATM, SDS-PAGE | Homo sapiens |
More | dimer formation is specific to the PEX domain of MT1-MMP, the PEX domain of MT4-MMP does not substitute for it | Homo sapiens |
oligomer | 1 * 50000, mutant MT1EADELTATM, SDS-PAGE | Homo sapiens |
Synonyms | Comment | Organism |
---|---|---|
MT-MMP1 | - |
Homo sapiens |
General Information | Comment | Organism |
---|---|---|
physiological function | MT-MMP1 must form a homophilic ternary complex with TIMP-2 and pro-MMP-2 to activate MMP-2 | Homo sapiens |