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Literature summary for 3.4.24.B5 extracted from

  • Morrison, C.J.; Overall, C.M.
    TIMP independence of matrix metalloproteinase (MMP)-2 activation by membrane type 2 (MT2)-MMP is determined by contributions of both the MT2-MMP catalytic and hemopexin C domains (2006), J. Biol. Chem., 281, 26528-26539.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
Collagen enhances MMP-2 activation by MT2-MMP Homo sapiens
additional information TIMPs 1-4 and claudin-5 do not enhance MMP-2 activation by MT2-MMP Homo sapiens

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli and in Timp2-/- skin fibroblasts Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
TIMP-2 inhibitory above 10 nM Homo sapiens

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
31400
-
recombinant form of the MT2-MMP hemopexin C domain with linker Homo sapiens
66000
-
fully active enzyme, SDS-PAGE Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Purification (Commentary)

Purification (Comment) Organism
Ni2+-chelate column chromatography, CM-Sepharose column chromatography, and Q Sepharose column cromatography Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
pro-form of matrix metalloproteinase 2 + H2O MMP-2 hemopexin carboxyl domain-dependent activation process Homo sapiens active form of matrix metalloproteinase 2
-
?
Type I collagen + H2O weak collagenase activity Homo sapiens ?
-
?

Synonyms

Synonyms Comment Organism
membrane type 2 matrix metalloproteinase
-
Homo sapiens
MMP-15
-
Homo sapiens
MT2-MMP
-
Homo sapiens