Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.4.24.24 extracted from

  • Monaco, S.; Gioia, M.; Rodriguez, J.; Fasciglione, G.F.; Di Pierro, D.; Lupidi, G.; Krippahl, L.; Marini, S.; Coletta, M.
    Modulation of the proteolytic activity of matrix metalloproteinase-2 (gelatinase A) on fibrinogen (2007), Biochem. J., 402, 503-513.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.24.24

Inhibitors

Inhibitors Comment Organism Structure
batimastat i.e. BB-94, a peptidomimetic inhibitor Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information kinetics of trunacted enzyme and modified fibrinogen substrates, Michaelis-Menten mechanism, overview Homo sapiens
0.159
-
 fibrinogen cleavage of the alpha-chain of the native substrate, full-length MMP-2, pH 7.1, 37°C Homo sapiens

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+
-
 Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
Fibrinogen + H2O Homo sapiens
-
 ?
-
 ?
Gelatin + H2O Homo sapiens
-
 ?
-
 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(7-methoxycoumarin-4-yl)acetyl-Pro-Leu-Gly-Leu-2,6-diaminopimelyl-Ala-Arg-NH2 + H2O
-
 Homo sapiens ?
-
 ?
Bovine fibrinogen + H2O proteolytic processing of bovine fibrinogen bringing about the formation of a product unable to form fibrin clots, preferential binding of MMP-2 to the beta-chain of fibrinogen through its haemopexin-like domain, removal of the domain dramatically alters the proteolytic reaction mechanism, molecular docking and modelling, overview Homo sapiens ?
-
 ?
Fibrinogen + H2O
-
 Homo sapiens ?
-
 ?
Gelatin + H2O
-
 Homo sapiens ?
-
 ?
Gelatin + H2O gelatin zymography Homo sapiens ?
-
 ?
peroxynitrite-treated fibrinogen + H2O
-
 Homo sapiens ?
-
 ?

Subunits

Subunits Comment Organism
More modeling of the interaction of fibrinogen with different truncated forms of MMP-2, i.e. the autoinhibitory procatalytic domain, the catalytic domain, the catalytic domain lacking the fibronectin-like domain, the fibronectin-like domain alone, and the haemopexin-like domain, using crystal structures isolated from the full-length proMMP-2, PDB ID 1CK7, overview Homo sapiens

Synonyms

Synonyms Comment Organism
gelatinase A
-
 Homo sapiens
matrix metalloproteinase-2
-
 Homo sapiens
MMP-2
-
 Homo sapiens

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Homo sapiens

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
36.4
-
 fibrinogen cleavage of the alpha-chain of the native substrate, full-length MMP-2, pH 7.1, 37°C Homo sapiens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.2
-
-
 Homo sapiens

pH Range

pH Minimum pH Maximum Comment Organism
6 9.3 activity range, pH-dependence of catalytic parameters for MMP-2 on fibrinogen, pH-dependence of the rate-limiting step shows a bell-shaped profile, overview Homo sapiens