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Literature summary for 3.4.24.80 extracted from

  • Gioia, M.; Fasciglione, G.F.; Monaco, S.; Iundusi, R.; Sbardella, D.; Marini, S.; Tarantino, U.; Coletta, M.
    pH dependence of the enzymatic processing of collagen I by MMP-1 (fibroblast collagenase), MMP-2 (gelatinase A), and MMP-14 ectodomain (2010), J. Biol. Inorg. Chem., 15, 1219-1232.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
batimastat
-
Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.00025
-
collagen type I alpha-2 chain 1-protonated enzyme, 50 mM Tris-HCl, 0.1 M NaCl, 10 mM CaCl2 plus 0.05% Brij 35,at pH 7.3 and 37°C Homo sapiens
0.0003
-
collagen I alpha-1 chain pH not specified in the publication, 37°C, MMP-1: 1-protonated Homo sapiens
0.00065
-
collagen I alpha-2 chain pH not specified in the publication, 37°C, MMP-1: 3-protonated Homo sapiens
0.00077
-
collagen I alpha-1 chain pH not specified in the publication, 37°C, MMP-1: 2-protonated Homo sapiens
0.00086
-
collagen type I alpha-1 chain 1-protonated enzyme, 50 mM Tris-HCl, 0.1 M NaCl, 10 mM CaCl2 plus 0.05% Brij 35,at pH 7.3 and 37°C Homo sapiens
0.0027
-
collagen I alpha-1 chain pH not specified in the publication, 37°C, MMP-1: 0-protonated Homo sapiens
0.0031
-
collagen I alpha-2 chain pH not specified in the publication, 37°C, MMP-1: 0-protonated Homo sapiens
0.004
-
collagen type I alpha-2 chain 2-protonated enzyme, 50 mM Tris-HCl, 0.1 M NaCl, 10 mM CaCl2 plus 0.05% Brij 35,at pH 7.3 and 37°C Homo sapiens
0.0079
-
collagen I alpha-2 chain pH not specified in the publication, 37°C, MMP-1: 1-protonated Homo sapiens
0.045
-
collagen type I alpha-1 chain 0-protonated enzyme, 50 mM Tris-HCl, 0.1 M NaCl, 10 mM CaCl2 plus 0.05% Brij 35,at pH 7.3 and 37°C Homo sapiens
0.12
-
collagen I alpha-2 chain pH not specified in the publication, 37°C, MMP-1: 2-protonated Homo sapiens
0.12
-
collagen type I alpha-1 chain 3-protonated enzyme, 50 mM Tris-HCl, 0.1 M NaCl, 10 mM CaCl2 plus 0.05% Brij 35,at pH 7.3 and 37°C Homo sapiens
0.14
-
collagen type I alpha-2 chain 3-protonated enzyme, 50 mM Tris-HCl, 0.1 M NaCl, 10 mM CaCl2 plus 0.05% Brij 35,at pH 7.3 and 37°C Homo sapiens
0.17
-
collagen type I alpha-1 chain 2-protonated enzyme, 50 mM Tris-HCl, 0.1 M NaCl, 10 mM CaCl2 plus 0.05% Brij 35,at pH 7.3 and 37°C Homo sapiens
0.32
-
collagen I alpha-1 chain pH not specified in the publication, 37°C, MMP-1: 3-protonated Homo sapiens
0.53
-
collagen type I alpha-2 chain 0-protonated enzyme, 50 mM Tris-HCl, 0.1 M NaCl, 10 mM CaCl2 plus 0.05% Brij 35,at pH 7.3 and 37°C Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane
-
Homo sapiens 16020
-

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-cyclohexylalanine-Gly-norvaline-His-Ala-(N-3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-NH2 + H2O degradation of synthetic substrate is pH-independent Homo sapiens ?
-
?
(7-methoxycoumarin-4-yl)acetyl-Pro-Leu-Ala-Cys(p-OMeBz)-Trp-Ala-Arg(N-3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-NH2 + H2O
-
Homo sapiens ?
-
?
collagen I alpha-1 chain + H2O overall enzymatic activity is higher on the alpha-2 chain for both MMP-1 and MMP-2. In MMP-2 a marked difference for substrate affinity (higher for the alpha-1 chain) is overwhelmed by an even more marked propensity to cleave the alpha-2 chain Homo sapiens ?
-
?
collagen I alpha-2 chain + H2O overall enzymatic activity is higher on the alpha-2 chain for both MMP-1 and MMP-2. In MMP-2 a marked difference for substrate affinity (higher for the alpha-1 chain) is overwhelmed by an even more marked propensity to cleave the alpha-2 chain Homo sapiens ?
-
?
collagen type I alpha-1 chain + H2O the MMP-14 ectodomain preferentially cleaves the alpha-1 chain of collagen type I Homo sapiens ?
-
?
collagen type I alpha-2 chain + H2O
-
Homo sapiens ?
-
?

Synonyms

Synonyms Comment Organism
gelatinase A
-
Homo sapiens
matrix metalloproteinase 14
-
Homo sapiens
MMP-14
-
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
0.0089
-
collagen type I alpha-2 chain 1-protonated enzyme, 50 mM Tris-HCl, 0.1 M NaCl, 10 mM CaCl2 plus 0.05% Brij 35,at pH 7.3 and 37°C Homo sapiens
0.014
-
collagen type I alpha-2 chain 2-protonated enzyme, 50 mM Tris-HCl, 0.1 M NaCl, 10 mM CaCl2 plus 0.05% Brij 35,at pH 7.3 and 37°C Homo sapiens
0.019
-
collagen I alpha-1 chain pH not specified in the publication, 37°C, MMP-1: 1-protonated Homo sapiens
0.3
-
collagen type I alpha-1 chain 1-protonated enzyme, 50 mM Tris-HCl, 0.1 M NaCl, 10 mM CaCl2 plus 0.05% Brij 35,at pH 7.3 and 37°C Homo sapiens
0.43
-
collagen type I alpha-1 chain 2-protonated enzyme, 50 mM Tris-HCl, 0.1 M NaCl, 10 mM CaCl2 plus 0.05% Brij 35,at pH 7.3 and 37°C Homo sapiens
0.47
-
collagen I alpha-1 chain pH not specified in the publication, 37°C, MMP-1: 0-protonated Homo sapiens
0.68
-
collagen I alpha-1 chain pH not specified in the publication, 37°C, MMP-1: 2-protonated Homo sapiens
1.1
-
collagen I alpha-1 chain pH not specified in the publication, 37°C, MMP-1: 3-protonated Homo sapiens
1.52
-
collagen I alpha-2 chain pH not specified in the publication, 37°C, MMP-1: 3-protonated Homo sapiens
4.09
-
collagen type I alpha-2 chain 4-protonated enzyme, 50 mM Tris-HCl, 0.1 M NaCl, 10 mM CaCl2 plus 0.05% Brij 35,at pH 7.3 and 37°C Homo sapiens
4.56
-
collagen type I alpha-1 chain 0-protonated enzyme, 50 mM Tris-HCl, 0.1 M NaCl, 10 mM CaCl2 plus 0.05% Brij 35,at pH 7.3 and 37°C Homo sapiens
5.79
-
collagen I alpha-2 chain pH not specified in the publication, 37°C, MMP-1: 1-protonated Homo sapiens
9.89
-
collagen I alpha-2 chain pH not specified in the publication, 37°C, MMP-1: 0-protonated Homo sapiens
10.41
-
collagen type I alpha-1 chain 4-protonated enzyme, 50 mM Tris-HCl, 0.1 M NaCl, 10 mM CaCl2 plus 0.05% Brij 35,at pH 7.3 and 37°C Homo sapiens
58.61
-
collagen type I alpha-2 chain 0-protonated enzyme, 50 mM Tris-HCl, 0.1 M NaCl, 10 mM CaCl2 plus 0.05% Brij 35,at pH 7.3 and 37°C Homo sapiens
255.6
-
collagen I alpha-2 chain pH not specified in the publication, 37°C, MMP-1: 2-protonated Homo sapiens

pH Range

pH Minimum pH Maximum Comment Organism
6 9.2 degradation of collagen I: over the whole pH range investigated the enzymatic activity toward the alpha-2 chain is significantly higher than that toward the alpha-1 chain. Difference is maximal at alkaline pH (being about 20fold at pH 9.2) and it decreases at neutral pH, such that at pH 7.3 the enzymatic processing of the alpha-2 chain is only about 5fold higher than for the alpha-1 chain Homo sapiens

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
2.5
-
collagen type I alpha-1 chain 2-protonated enzyme, 50 mM Tris-HCl, 0.1 M NaCl, 10 mM CaCl2 plus 0.05% Brij 35,at pH 7.3 and 37°C Homo sapiens
3.4
-
collagen I alpha-1 chain pH not specified in the publication, 37°C, MMP-1: 3-protonated Homo sapiens
3.5
-
collagen type I alpha-2 chain 2-protonated enzyme, 50 mM Tris-HCl, 0.1 M NaCl, 10 mM CaCl2 plus 0.05% Brij 35,at pH 7.3 and 37°C Homo sapiens
30
-
collagen type I alpha-2 chain 4-protonated enzyme, 50 mM Tris-HCl, 0.1 M NaCl, 10 mM CaCl2 plus 0.05% Brij 35,at pH 7.3 and 37°C Homo sapiens
63
-
collagen I alpha-1 chain pH not specified in the publication, 37°C, MMP-1: 1-protonated Homo sapiens
88
-
collagen type I alpha-1 chain 4-protonated enzyme, 50 mM Tris-HCl, 0.1 M NaCl, 10 mM CaCl2 plus 0.05% Brij 35,at pH 7.3 and 37°C Homo sapiens
100
-
collagen type I alpha-1 chain O-protonated enzyme, 50 mM Tris-HCl, 0.1 M NaCl, 10 mM CaCl2 plus 0.05% Brij 35,at pH 7.3 and 37°C Homo sapiens
110
-
collagen type I alpha-2 chain O-protonated enzyme, 50 mM Tris-HCl, 0.1 M NaCl, 10 mM CaCl2 plus 0.05% Brij 35,at pH 7.3 and 37°C Homo sapiens
170
-
collagen I alpha-1 chain pH not specified in the publication, 37°C, MMP-1: 0-protonated Homo sapiens
350
-
collagen type I alpha-2 chain 1-protonated enzyme, 50 mM Tris-HCl, 0.1 M NaCl, 10 mM CaCl2 plus 0.05% Brij 35,at pH 7.3 and 37°C Homo sapiens
360
-
collagen type I alpha-1 chain 1-protonated enzyme, 50 mM Tris-HCl, 0.1 M NaCl, 10 mM CaCl2 plus 0.05% Brij 35,at pH 7.3 and 37°C Homo sapiens
730
-
collagen I alpha-2 chain pH not specified in the publication, 37°C, MMP-1: 1-protonated Homo sapiens
880
-
collagen I alpha-1 chain pH not specified in the publication, 37°C, MMP-1: 2-protonated Homo sapiens
2100
-
collagen I alpha-2 chain pH not specified in the publication, 37°C, MMP-1: 2-protonated Homo sapiens
2300
-
collagen I alpha-2 chain pH not specified in the publication, 37°C, MMP-1: 3-protonated Homo sapiens
3200
-
collagen I alpha-2 chain pH not specified in the publication, 37°C, MMP-1: 0-protonated Homo sapiens