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Literature summary for 3.4.24.23 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

Activating Compound Comment Organism Structure
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
additional information cholesterol, dehydroepiandrosterone sulfate, and heparin do not affect MMP-7-catalyzed degradations of fibronactin and laminin-332 Homo sapiens

Protein Variants

Protein Variants Comment Organism
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

Inhibitors Comment Organism Structure
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

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

Metals/Ions

Metals/Ions Comment Organism Structure
additional information metalloprotease Homo sapiens

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
Colo-201 cell
-
Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(7-methoxycoumarin-4-yl)-acetyl-Pro-Leu-Gly-Leu-[N-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl]-Ala-Arg amide + H2O
-
Homo sapiens ?
-
?
Fibronectin + H2O also MMP-7-catalyzed cleavages of chymotryptic fragments of fibronectin by cell-bound MMP-7, overview Homo sapiens ?
-
?
Fibronectin + H2O pericellular substrate Homo sapiens ?
-
?
kappa-casein + H2O
-
Homo sapiens ?
-
?
laminin-332 + H2O
-
Homo sapiens ? analysis of peptide fragment degradation products ?
laminin-332 + H2O pericellular substrate Homo sapiens ?
-
?
additional information binding of MMP-7 to EJ-1 cell surface Homo sapiens ?
-
?
additional information immunohistochemic analysis of peptide fragment degradation products 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
37
-
assay at Homo sapiens

pH Optimum

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

General Information

General Information Comment Organism
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