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Literature summary for 3.4.24.80 extracted from
- Solvent water interactions within the active site of the membrane type I matrix metalloproteinase (2017), Phys. Chem. Chem. Phys., 19, 30316-30331 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene MMP14, recombinant expression of C-terminally His-tagged wild-type and mutant Co2+-MT1-MMPs and apoenzymes in Escherichia coli strain BL21(DE3), the plasmid contains the catalytic domain of human MT1-MMP together with the hinge linker to the hemopexin-like domain (residues 112-292). Interaction of the His-tag with the protein cleft, modelling, overview | Homo sapiens |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| purified recombinant His-tagged apoenzyme and Zn2+-MT1-MMP, X-ray diffraction structure determination and analysis at 2.24-2.88 A resolution, modelling with bound substrate peptide IAG | Homo sapiens |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| C127S | site-directed mutagenesis, no significant difference in activity is observed for the mutant C127S and the wild-type MT1-MMP | Homo sapiens |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| Acetohydroxamic acid | inhibition of Co2+-MT1-MMP | Homo sapiens |  |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Ca2+ | enzyme-bound | Homo sapiens | |
| additional information | preparation of apo-MT1-MMP (metal-free material) and preparation of Co2+-MT1-MMP. Co2+-MMP-1 is obtained by removal of the native metal dialyzing against o-phenanthroline and successively addition of cobalt salt, method overview | Homo sapiens | |
| Zn2+ | zinc-dependent endopeptidase, Zn2+ has a catalytic function | Homo sapiens | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | P50281 | - |
- |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| proteolytic modification | the enzyme performs autoproteolysis | Homo sapiens |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant C-terminally His-tagged wild-type and mutant Co2+-MT1-MMPs and apoenzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and ultrafiltration | Homo sapiens |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | the enzyme performs autoproteolysis | Homo sapiens | ? | - |
? | |
| peptide IAG + H2O | enzyme binding structure, modelling, overview | Homo sapiens | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| membrane type I MMP | - |
Homo sapiens |
| MMP-14 | - |
Homo sapiens |
| MT1-MMP | - |
Homo sapiens |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 25 | - |
assay at | Homo sapiens |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.4 | - |
assay at | Homo sapiens |
General Information
| General Information | Comment | Organism |
|---|---|---|
| metabolism | matrix metalloproteinases (MMP) are an important family of proteases which catalyze the degradation of extracellular matrix components | Homo sapiens |
| additional information | solvent water interactions within the active site of the membrane type I matrix metalloproteinase, crystal structure analysis, quantum mechanics/molecular mechanics geometries and modelling, structure modelling, overview | Homo sapiens |
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Release 2023.1 (January 2023)
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