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Literature summary for 3.4.24.24 extracted from

  • Koo, B.H.; Han, J.H.; Yeom, Y.I.; Kim, D.S.
    Thrombin-dependent MMP-2 activity is regulated by heparan sulfate (2010), J. Biol. Chem., 285, 41270-41279.
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
heparan sulfate essential for thrombin-mediated activation of pro-MMP-2 Homo sapiens
syndecan-1 expression of syndecan-1 increases thrombin-mediated activation of pro-MMP-2 in K562 cells Homo sapiens
thrombin dependent on, molecular mechanisms underlying thrombin-mediated MMP-2 activation, overview. Interaction of MMP-2 with exosites 1 and 2 of thrombin is crucial for thrombin- mediated MMP-2 degradation, and inhibition of this interaction by heparan sulfate or hirudin fragment results in a decrease in MMP-2 degradation, interaction between exosite 1 and hemopexin-like domain of MMP-2 Homo sapiens

Cloned(Commentary)

Cloned (Comment) Organism
expression of His- and myc-tagged pro-MMP-2 Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
additional information simultaneous binding of each ligand heparan sulfate and hirudin to the exosites is necessary for the complete inhibition of MMP-2 degradation by thrombin Homo sapiens

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ dependent on Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
K-562 cell
-
Homo sapiens
-

Synonyms

Synonyms Comment Organism
matrix metalloprotease 2
-
Homo sapiens
MMP-2
-
Homo sapiens

General Information

General Information Comment Organism
additional information thrombin-dependent MMP-2 activity is regulated by heparan sulfate, molecular mechanism, regulatory role of hemopexin-like domain in MMP-2 degradation, overview Homo sapiens