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Literature summary for 3.4.24.23 extracted from

  • Yamamoto, K.; Miyazaki, K.; Higashi, S.
    Pericellular proteolysis by matrix metalloproteinase-7 is differentially modulated by cholesterol sulfate, sulfatide, and cardiolipin (2014), FEBS J., 281, 3346-3356.
    View publication on PubMed
Search for more literature for 3.4.24.23

Activating Compound

Activating Compound Comment Organism Structure
additional information the enzyme bound to cell surface sulfatide or cholesterol sulfate cleaves specific cell surface proteins and releases similar fragments, whereas the cleavage is not stimulated by cell surface cardiolipin-bound enzyme Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
cardiolipin associates with the enzyme at the cell surface and inhibits by 92% Homo sapiens
Cholesterol sulfate associates with the enzyme st the cell surface and modulates the substrate preference of the enzyme, 20% inhibition Homo sapiens
additional information the internal four residues Ile29, Arg33, Arg51 and Trp55 of MMP-7 are important for binding of inhibitory acidic lipids, overview Homo sapiens
Sulfatide associates with the enzyme at the cell surface and inhibits by 80% Homo sapiens
TAPI-1 a hydroxamate-based matrix metalloproteinase inhibitor, reduces the affinity of the enzyme for cholesterol sulfate and cardiolipin, but not for sulfatide, molecular mechanism by which TAPI-1 inhibits binding of MMP-7 to the lipids, overview Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular the enzyme is secreted Homo sapiens
-
-
additional information the enzyme potentially associates with the cell surface via sulfatide and cardiolipin when they are overexpressed on the cell surface, molecular interaction, overview Homo sapiens
-
-

Organism

Organism UniProt Comment Textmining
Homo sapiens P09237
-
-

Source Tissue

Source Tissue Comment Organism Textmining
commercial preparation recombinant enzyme Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
fibronecin + H2O pericellular proteolysis Homo sapiens ?
-
 ?
kappa-casein + H2O
-
 Homo sapiens ?
-
 ?
laminin-332 + H2O pericellular proteolysis Homo sapiens ?
-
 ?
additional information cholesterol sulfate modulates the substrate preference of the enzyme, thereby regulating its pericellular proteolytic action Homo sapiens ?
-
 ?

Synonyms

Synonyms Comment Organism
Matrix metalloproteinase-7
-
 Homo sapiens
MMP-7
-
 Homo sapiens

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25 37 assay at Homo sapiens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5 8 assay at Homo sapiens

IC50 Value

IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
0.0006
-
 pH 8.0, 25°C Homo sapiens cardiolipin
0.0007
-
 pH not specified in the publication, 37°C Homo sapiens Sulfatide

General Information

General Information Comment Organism
additional information the enzyme potentially associates with the cell surface via sulfatide and cardiolipin when they are overexpressed on the cell surface, molecular interaction, overview. The internal four residues Ile29, Arg33, Arg51 and Trp55 of MMP-7 are important for binding of inhibitory acidic lipids, overview Homo sapiens
physiological function matrix metalloproteinases take part in tumor invasion and metastasis through modification of the biological functions of various cell surface proteins and degradation of extracellular matrix proteins. Acidic lipids differentially regulate pericellular proteolysis by MMP-7 through allosteric alteration of the substrate-binding site and their inherent affinities for MMP-7 substrates, overview Homo sapiens