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Literature summary extracted from

  • Yamamoto, K.; Miyazaki, K.; Higashi, S.
    Cholesterol sulfate alters substrate preference of matrix metalloproteinase-7 and promotes degradations of pericellular laminin-332 and fibronectin (2010), J. Biol. Chem., 285, 28862-28873.
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.4.24.23 Cholesterol sulfate selectively alters substrate preference of matrix metalloproteinase-7 and promotes degradations of pericellular laminin-332 and fibronectin. Degradation of laminin-332 (laminin-5) catalyzed by MMP-7 is accelerated dramatically in the presence of cholesterol sulfate, whereas the sulfated lipid inhibits the degradation of casein catalyzed by the protease. Cholesterol sulfate facilitates the proteolyses by cross-linking MMP-7 to its substrates, mechanism, overview Homo sapiens
3.4.24.23 additional information cholesterol, dehydroepiandrosterone sulfate, and heparin do not affect MMP-7-catalyzed degradations of fibronactin and laminin-332 Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
3.4.24.23 additional information MMP-7 tethered to cancer cell surface via cholesterol sulfate degrades fibronectin and laminin-332 coated on a culture plate Homo sapiens

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.24.23 N-{(2R)-2-[2-(hydroxyamino)-2-oxoethyl]-4-methylpentanoyl}-3-(naphthalen-2-yl)-L-alanyl-N-(2-aminoethyl)-L-alaninamide i.e. TAPI-1, a hydroxamate-based metalloproteinase inhibitor Homo sapiens

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.4.24.23 cell surface the enzyme is secreted Homo sapiens 9986
-
3.4.24.23 extracellular the enzyme is secreted Homo sapiens
-
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.4.24.23 additional information metalloprotease Homo sapiens

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.4.24.23 Fibronectin + H2O Homo sapiens also MMP-7-catalyzed cleavages of chymotryptic fragments of fibronectin by cell-bound MMP-7, overview ?
-
 ?
3.4.24.23 laminin-332 + H2O Homo sapiens pericellular substrate ?
-
 ?
3.4.24.23 additional information Homo sapiens binding of MMP-7 to EJ-1 cell surface ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.4.24.23 Homo sapiens
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.4.24.23 Colo-201 cell
-
 Homo sapiens
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.24.23 (7-methoxycoumarin-4-yl)-acetyl-Pro-Leu-Gly-Leu-[N-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl]-Ala-Arg amide + H2O
-
 Homo sapiens ?
-
 ?
3.4.24.23 Fibronectin + H2O also MMP-7-catalyzed cleavages of chymotryptic fragments of fibronectin by cell-bound MMP-7, overview Homo sapiens ?
-
 ?
3.4.24.23 Fibronectin + H2O pericellular substrate Homo sapiens ?
-
 ?
3.4.24.23 kappa-casein + H2O
-
 Homo sapiens ?
-
 ?
3.4.24.23 laminin-332 + H2O
-
 Homo sapiens ? analysis of peptide fragment degradation products ?
3.4.24.23 laminin-332 + H2O pericellular substrate Homo sapiens ?
-
 ?
3.4.24.23 additional information binding of MMP-7 to EJ-1 cell surface Homo sapiens ?
-
 ?
3.4.24.23 additional information immunohistochemic analysis of peptide fragment degradation products Homo sapiens ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.4.24.23 Matrix metalloproteinase-7
-
 Homo sapiens
3.4.24.23 MMP-7
-
 Homo sapiens

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.4.24.23 37
-
 assay at Homo sapiens

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.4.24.23 7.5
-
 assay at Homo sapiens

General Information

EC Number General Information Comment Organism
3.4.24.23 physiological function binding of MMP-7 to cell surface cholesterol sulfate is essential for the cell membrane-associated proteolytic action of MMP-7 thereby ECM, thereby. Degradation of laminin-332 (laminin-5) catalyzed by MMP-7 is accelerated dramatically in the presence of cholesterol sulfate, whereas the sulfated lipid inhibits the degradation of casein catalyzed by the protease. Cholesterol sulfate facilitates the proteolyses by cross-linking MMP-7 to its substrates, mechanism, overview Homo sapiens