Activating Compound | Comment | Organism | Structure |
---|---|---|---|
additional information | purified proMMP-10-catalytic domain is activated overnight in the presence of the organomercurial compound 4-aminophenyl mercuric acetate | Homo sapiens |
Crystallization (Comment) | Organism |
---|---|
purified isolated catalytic enzyme domain in complex with inhibitor TIMP1, 1:1.2 (mol/mol) mixture of enzyme protein and fully deglycosylated TIMP-N30A mutant is concentrated to achieve a final protein concentration of 4-5 mg/ml. Crystals are grown by hanging drop vapor diffusion method at room temperature in 0.1 M sodium dihydrogen phosphate, pH 6.5, 12% w/v PEG 8000, 2 weeks, X-ray diffraction structure determination and analysis at 1.9 A resolution, molecular replacement | Homo sapiens |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
tissue inhibitor of metalloproteinases 1 | TIMP-1, the protein is expressed in HEK 293E cells, enzyme binding structure analysis and mechanism of inhibition, detailed overview and comparison to stromelysin-1, EC 3.4.24.17 | Homo sapiens | |
tissue inhibitor of metalloproteinases 2 | TIMP-2, the protein is expressed in HEK 293E cells | Homo sapiens |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
extracellular | a secreted metalloproteinase | Homo sapiens | - |
- |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Zn2+ | the active site of the domain possesses the conserved zinc-binding motif HEXXHXXGXXH, in which the imidazole side chains of His217, His221, and His227 coordinate the catalytic zinc ion | Homo sapiens |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | Homo sapiens | the enzyme degrades a variety of extracellular matrix proteins, including collagen types III-V and fibronectin, and also activate other proteases, including MMP-1, MMP-7, MMP-8, and MMP-9 | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | P01033 | - |
- |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
lung | - |
Homo sapiens | - |
lung cancer cell | - |
Homo sapiens | - |
skeletal muscle | - |
Homo sapiens | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
Ac-Pro-Leu-Gly-(2-mercapto-4-methyl-pentanoyl)-Leu-Gly-OC2H5 + H2O | - |
Homo sapiens | ? | - |
? | |
additional information | the enzyme degrades a variety of extracellular matrix proteins, including collagen types III-V and fibronectin, and also activate other proteases, including MMP-1, MMP-7, MMP-8, and MMP-9 | Homo sapiens | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
Matrix metalloproteinase-10 | - |
Homo sapiens |
MMP-10 | - |
Homo sapiens |
stromelysin-2 | - |
Homo sapiens |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Homo sapiens |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7 | - |
assay at | Homo sapiens |
Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | inhibition kinetics using the isolated enzyme's catalytic domain, overview | Homo sapiens | |
0.0000011 | - |
tissue inhibitor of metalloproteinases 1 | catalytic enzyme domain, pH 7.0, 37°C | Homo sapiens | |
0.0000058 | - |
tissue inhibitor of metalloproteinases 2 | catalytic enzyme domain, pH 7.0, 37°C | Homo sapiens |
General Information | Comment | Organism |
---|---|---|
evolution | despite their similar substrate specificities, the stromelysins show differential patterns of transcriptional regulation and tissue distribution that hint at distinct physiological functions in processes such as skeletal development, wound healing, and vascular remodeling | Homo sapiens |
additional information | the active site of the domain possesses the conserved zinc-binding motif HEXXHXXGXXH, in which the imidazole side chains of His217, His221, and His227 coordinate the catalytic zinc ion, and Glu218 is positioned to function as a general acid/base in the hydrolysis reaction | Homo sapiens |
physiological function | the enzyme functions in skeletal development, wound healing, and vascular remodeling. It is also implicated in lung tumorigenesis and tumor progression. Regulation of enzyme MMP-10 by tissue inhibitors of metalloproteinases | Homo sapiens |