Literature summary extracted from
Decaneto, E.; Vasilevskaya, T.; Kutin, Y.; Ogata, H.; Grossman, M.; Sagi, I.; Havenith, M.; Lubitz, W.; Thiel, W.; Cox, N.
Solvent water interactions within the active site of the membrane type I matrix metalloproteinase (2017), Phys. Chem. Chem. Phys., 19, 30316-30331 .
Cloned(Commentary)
EC Number |
Cloned (Comment) |
Organism |
---|
3.4.24.80 |
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)
EC Number |
Crystallization (Comment) |
Organism |
---|
3.4.24.80 |
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
EC Number |
Protein Variants |
Comment |
Organism |
---|
3.4.24.80 |
C127S |
site-directed mutagenesis, no significant difference in activity is observed for the mutant C127S and the wild-type MT1-MMP |
Homo sapiens |
Inhibitors
EC Number |
Inhibitors |
Comment |
Organism |
Structure |
---|
3.4.24.80 |
Acetohydroxamic acid |
inhibition of Co2+-MT1-MMP |
Homo sapiens |
|
Metals/Ions
EC Number |
Metals/Ions |
Comment |
Organism |
Structure |
---|
3.4.24.80 |
Ca2+ |
enzyme-bound |
Homo sapiens |
|
3.4.24.80 |
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 |
|
3.4.24.80 |
Zn2+ |
zinc-dependent endopeptidase, Zn2+ has a catalytic function |
Homo sapiens |
|
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
3.4.24.80 |
Homo sapiens |
P50281 |
- |
- |
Posttranslational Modification
EC Number |
Posttranslational Modification |
Comment |
Organism |
---|
3.4.24.80 |
proteolytic modification |
the enzyme performs autoproteolysis |
Homo sapiens |
Purification (Commentary)
EC Number |
Purification (Comment) |
Organism |
---|
3.4.24.80 |
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)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
3.4.24.80 |
additional information |
the enzyme performs autoproteolysis |
Homo sapiens |
? |
- |
? |
|
3.4.24.80 |
peptide IAG + H2O |
enzyme binding structure, modelling, overview |
Homo sapiens |
? |
- |
? |
|
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
3.4.24.80 |
membrane type I MMP |
- |
Homo sapiens |
3.4.24.80 |
MMP-14 |
- |
Homo sapiens |
3.4.24.80 |
MT1-MMP |
- |
Homo sapiens |
Temperature Optimum [°C]
EC Number |
Temperature Optimum [°C] |
Temperature Optimum Maximum [°C] |
Comment |
Organism |
---|
3.4.24.80 |
25 |
- |
assay at |
Homo sapiens |
pH Optimum
EC Number |
pH Optimum Minimum |
pH Optimum Maximum |
Comment |
Organism |
---|
3.4.24.80 |
7.4 |
- |
assay at |
Homo sapiens |
General Information
EC Number |
General Information |
Comment |
Organism |
---|
3.4.24.80 |
metabolism |
matrix metalloproteinases (MMP) are an important family of proteases which catalyze the degradation of extracellular matrix components |
Homo sapiens |
3.4.24.80 |
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 |