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Literature summary for 3.4.24.23 extracted from

  • Prior, S.H.; Fulcher, Y.G.; Koppisetti, R.K.; Jurkevich, A.; Van Doren, S.R.
    Charge-triggered membrane insertion of matrix metalloproteinase-7, supporter of innate immunity and tumors (2015), Structure, 23, 2099-2110 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.24.23

Inhibitors

Inhibitors Comment Organism Structure
additional information the enzyme contains an auto-inhibitory peptide Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular the enzyme is secreted Homo sapiens
-
-
plasma membrane charge-triggered membrane insertion of matrix metalloproteinase-7. Binding to cholesterol sulfate partially embeds the protease in the bilayer, restricts its diffusion, and tips the active site away from the bilayer. Its insertion of hydrophobic residues organizes the lipids, pushing the head groups and sterol sulfate outward towards the enzyme's positive charge on the periphery of the enlarged interface. Fluorescence probing demonstrates a similar mode of binding to plasma membranes and internalized vesicles of colon cancer cells. Binding of bilayered micelles induces allosteric activation and conformational change in the auto-inhibitory peptide and the adjacent scissile site, illustrating a potential intermediate in the activation of the zymogen. Cholesterol sulfate reorients and inserts proMMP-7 into bicelles. Potential interactions of the II-III loop and interdomain linker with bilayer, NMR structure determination and analysis, overview Homo sapiens 5886
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Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ a zinc-dependent metalloproteinase Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
heparin-binding epidermal growth factor precursor + H2O Homo sapiens
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 heparin-binding epidermal growth factor + HB-EGF pro-peptide
-
 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens P09237
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification binding of bilayered micelles induces allosteric activation and conformational change in the auto-inhibitory peptide and the adjacent scissile site, illustrating a potential intermediate in the activation of the zymogen Homo sapiens

Source Tissue

Source Tissue Comment Organism Textmining
Colo-205 cell
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 Homo sapiens
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colonic adenocarcinoma cell
-
 Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
heparin-binding epidermal growth factor precursor + H2O
-
 Homo sapiens heparin-binding epidermal growth factor + HB-EGF pro-peptide
-
 ?

Synonyms

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

General Information

General Information Comment Organism
additional information determination of NMR structures of the proMMP-7 zymogen free in solution and bound to membrane mimics, as well as by probing with a membrane-responsive fluor. Binding of plasma membranes and internalization, and bicelle-induced removal of auto-inhibitory conformation, overview Homo sapiens
physiological function matrix metalloproteinase-7 (MMP-7) sheds signaling proteins from cell surfaces to activate bacterial killing, wound healing, and tumorigenesis, mechanism targeting soluble MMP-7 to membranes. MMP-7 regulates the remodeling of female reproductive organs by proteolytic activation of heparin-binding epidermal growth factor precursor (pro-HB-EGF) to activate its ErbB4 receptor in uterine and mammary epithelia and tumor cells Homo sapiens