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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 .
    View publication on PubMed

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