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Literature summary for 3.4.24.23 extracted from

  • Ganguly, B.; Banerjee, J.; Elegbede, A.I.; Klocke, D.J.; Mallik, S.; Srivastava, D.K.
    Intrinsic selectivity in binding of matrix metalloproteinase-7 to differently charged lipid membranes (2007), FEBS Lett., 581, 5723-5726.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.24.23

Cloned(Commentary)

Cloned (Comment) Organism
overexpression of MMP-7 in Escherichia coli strain BL21(DE3) Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
additional information MMP-7 interacts with anionic, cationic and neutral lipid membranes, while the catalytic activity of the enzyme remains unaffected upon binding to neutral and negatively charged membranes, it is drastically impaired upon binding to the positively charged membranes, overview Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane MMP-7 interacts with anionic, cationic and neutral lipid membranes, it interacts strongest with anionic membranes, overview Homo sapiens 16020
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Organism

Organism UniProt Comment Textmining
Homo sapiens P09237
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-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(7-methoxycoumarin-4-yl)acetyl-Pro-Leu-Gly-Leu-N-3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl-Ala-Arg-NH2 + H2O
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 Homo sapiens ?
-
 ?
additional information MMP-7 interacts with anionic, cationic and neutral lipid membranes, it interacts strongest with anionic membranes, overview Homo sapiens ?
-
 ?

Subunits

Subunits Comment Organism
More bipolar distribution of the electrostatic surface potentials on the crystallographic structure of MMP-7, overview Homo sapiens

Synonyms

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