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Literature summary for 3.4.24.17 extracted from

  • Jerah, A.; Hobani, Y.; Kumar, B.V.; Bidwai, A.
    Curcumin binds in silico to anti-cancer drug target enzyme MMP-3 (human stromelysin-1) with affinity comparable to two known inhibitors of the enzyme (2015), Bioinformation, 11, 387-392 .
    View publication on PubMedView publication on EuropePMC
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Application

Application Comment Organism
drug development human enzyme MMP-3, i.e. stromelysin-1, is an anti-cancer drug target Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
5-methyl-5-(4-phenoxy-phenyl)-pyrimidine-2,4,6-trione MPPT, enzyme binding structure analysis Homo sapiens
curcumin i.e. 1,7-bis (4-hydroxy-3-methoxyphenol)-1,6-heptadiene-3,5-dione, molecular docking and prediction of binding interactions of curcumin with active site residues Homo sapiens
additional information interactions of curcumin with MMP-3 are compared to those of two known inhibitors of the enzyme, PBSA and MPPT, curcumin binds with affinity comparable to or better than the two known inhibitors Homo sapiens
[4-(4-phenyl-piperidin-1-yl)-benzenesulfonylamino]-acetic acid PBSA, enzyme binding structure analysis Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
 Homo sapiens
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ required, the catalytic domains contain Ca2+ ions Homo sapiens
Zn2+ a zinc metalloproteinase Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens P08254
-
-

Synonyms

Synonyms Comment Organism
MMP-3
-
 Homo sapiens
stromelysin-1
-
 Homo sapiens

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.000036
-
 curcumin pH and temperature not specified in the publication Homo sapiens
0.00005
-
 5-methyl-5-(4-phenoxy-phenyl)-pyrimidine-2,4,6-trione pH and temperature not specified in the publication Homo sapiens
0.000098
-
 [4-(4-phenyl-piperidin-1-yl)-benzenesulfonylamino]-acetic acid pH and temperature not specified in the publication Homo sapiens

General Information

General Information Comment Organism
additional information the active site of MMPs consists of two distinct regions: a groove in the protein surface, centered on the catalytic zinc ion and an S1 specificity site that varies considerably among members of the family. Bound inhibitors adopt extended conformations within the groove, make several hydrogen bonds with the enzyme and provide the fourth ligand for the catalytic zinc ion. The S1 subsite apparently plays a significant role in determining the substrate specificity in the active enzymes Homo sapiens