Information on EC 3.4.24.80 - membrane-type matrix metalloproteinase-1

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.4.24.80
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RECOMMENDED NAME
GeneOntology No.
membrane-type matrix metalloproteinase-1
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
endopeptidase activity. Activates progelatinase A by cleavage of the propeptide at Asn37-/-Leu. Other bonds hydrolysed include Gly35-/-Ile in the propeptide of collagenase 3, and Asn341-/-Phe, Asp441-/-Leu and Gln354-/-Thr in the aggrecan interglobular domain
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
cleavage of C-N-linkage
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hydrolysis
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CAS REGISTRY NUMBER
COMMENTARY hide
161384-17-4
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
rabbit
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Manually annotated by BRENDA team
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SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
((GP-4-hydroxy-L-proline)5GPK(7-methoxycoumarin-4-yl)acetyl)GPQGLRGQK(2,4-dinitrophenyl)GVR((GP-4-hydroxy-L-proline)5-NH2)3 + H2O
?
show the reaction diagram
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?
(7-methoxycoumarin-4-yl)-acetyl-L-Lys-Pro-Leu-Gly-Leu-Lys(N-3-(2,4-dinitrophenyl)-l-2,3-diaminopropionyl)-Ala-Arg-NH2 + H2O
?
show the reaction diagram
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-
-
-
?
(7-methoxycoumarin-4-yl)-acetyl-Pro-Leu-Ala-Cys(p-OmeBz)-Trp-Ala-Arg(Dpa)-NH2 + H2O
?
show the reaction diagram
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-
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?
(7-methoxycoumarin-4-yl)-acetyl-Pro-Leu-Gly-Leu-(3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-Ala-Arg-NH2 + H2O
(7-methoxycoumarin-4-yl)-acetyl-Pro-Leu-Gly + Leu-(3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-Ala-Arg-NH2
show the reaction diagram
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?
(7-methoxycoumarin-4-yl)acetyl-Arg-Pro-Lys-Pro-Tyr-Ala-Nva-Trp-Met-Lys-N-3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl-NH2 + H2O
?
show the reaction diagram
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-
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?
(7-methoxycoumarin-4-yl)acetyl-GTQGQEARGS-dinitrophenol NH2 + H2O
?
show the reaction diagram
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substrate covering the aggrecanase cleavage site of aggrecan
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?
(7-methoxycoumarin-4-yl)acetyl-L-Pro-Leu-Gly-Leu-(3-[2,4-dinitrophenyl]-L-2,3-diaminopropionyl)-Ala-Arg-NH2 + H2O
?
show the reaction diagram
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?
(7-methoxycoumarin-4-yl)acetyl-LAQAVRSSK-dinitrophenol NH2 + H2O
?
show the reaction diagram
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quenched fluorescent substrate mimicking the cleavage site of pro tumor necrosis factor alpha
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?
(7-methoxycoumarin-4-yl)acetyl-P-3-cyclohexylalanyl-norvalyl-HA-dinitrophenol NH2 + H2O
?
show the reaction diagram
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collagenase substrate
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?
(7-methoxycoumarin-4-yl)acetyl-Pro-cyclohexylalanine-Gly-norvaline-His-Ala-(N-3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-NH2 + H2O
?
show the reaction diagram
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degradation of synthetic substrate is pH-independent
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?
(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
?
show the reaction diagram
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?
(7-methoxycoumarin-4-yl)acetyl-Pro-Leu-Ala-Gln-Ala-Val-N-3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl-Arg-Ser-Ser-Arg-NH2 + H2O
?
show the reaction diagram
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?
(7-methoxycoumarin-4-yl)acetyl-Pro-Leu-Ala-Nva-N-3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl-Ala-Arg-NH2 + H2O
?
show the reaction diagram
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?
(7-methoxycoumarin-4-yl)acetyl-Pro-Leu-Gly-Leu-N-3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl-Ala-Arg-NH2 + H2O
?
show the reaction diagram
(7-methoxycoumarin-4-yl)acetyl-Pro-Lys-Pro-Leu-Ala-Leu-N-3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl-Ala-Arg-NH2 + H2O
?
show the reaction diagram
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?
aggrecan + H2O
?
show the reaction diagram
alpha subunit of low density lipoprotein receptor-related protein + H2O
?
show the reaction diagram
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?
alpha-1 microglobulin + H2O
?
show the reaction diagram
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?
alpha-2 macroglobulin + H2O
?
show the reaction diagram
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?
alpha-2-HS-glycoprotein + H2O
?
show the reaction diagram
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?
alpha1-antitrypsin + H2O
?
show the reaction diagram
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?
alpha1-proteinase inhibitor + H2O
?
show the reaction diagram
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?
alpha2-macroglobulin + H2O
?
show the reaction diagram
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?
alpha5 integrin + H2O
?
show the reaction diagram
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?
apolipoprotein A-I + H2O
?
show the reaction diagram
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?
apolipoprotein A-IV + H2O
?
show the reaction diagram
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?
apolipoprotein E + H2O
?
show the reaction diagram
apolipoprotein J + H2O
?
show the reaction diagram
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?
betaglycan + H2O
?
show the reaction diagram
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?
brain-specific angiogenesis inhibitor 1 + H2O
vasculostatin-120 + vasculostatin-40
show the reaction diagram
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the N terminus of BAI1 is cleaved extracellularly to generate a truncated receptor (vasculostatin-120) and a 40000 Da fragment (vasculostatin-40)
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?
casein + H2O
?
show the reaction diagram
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?
CD44 + H2O
?
show the reaction diagram
Collagen + H2O
?
show the reaction diagram
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?
collagen I + H2O
?
show the reaction diagram
collagen I alpha-1 chain + H2O
?
show the reaction diagram
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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
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?
collagen I alpha-2 chain + H2O
?
show the reaction diagram
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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
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?
collagen type I alpha-1 chain + H2O
?
show the reaction diagram
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the MMP-14 ectodomain preferentially cleaves the alpha-1 chain of collagen type I
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?
collagen type I alpha-2 chain + H2O
?
show the reaction diagram
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?
complement component 3 + H2O
?
show the reaction diagram
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?
cross-linked fibrin II + H2O
?
show the reaction diagram
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des-fibrinopeptides A and B, prepared by clotting fibrinogen with thrombin in the presence of factor XIIIa
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?
dermatan sulfate proteoglycan + H2O
?
show the reaction diagram
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?
E-cadherin + H2O
?
show the reaction diagram
Elastin + H2O
?
show the reaction diagram
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?
endoglin + H2O
soluble endoglin + ?
show the reaction diagram
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MMP-14 cleaves membrane-bound endoglin at a site in close proximity to the transmembrane domain between Gly586-Leu-587
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?
entactin + H2O
?
show the reaction diagram
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?
epidermal growth factor receptor + H2O
?
show the reaction diagram
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the enzyme plays a role in transactivation
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?
extracellular matrix metalloproteinase inducer + H2O
?
show the reaction diagram
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?
extracellular matrix metalloproteinase inducer + H2O
extracellular matrix metalloproteinase inducer fragment + ?
show the reaction diagram
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22000 Da in length
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?
F-gelatin + H2O
?
show the reaction diagram
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?
fibrillin + H2O
?
show the reaction diagram
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?
Fibrin + H2O
?
show the reaction diagram
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?
Fibrinogen + H2O
?
show the reaction diagram
fibroblast growth factor receptor-1 + H2O
?
show the reaction diagram
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?
fibroblast growth factor receptor-4 + H2O
?
show the reaction diagram
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?
Fibronectin + H2O
?
show the reaction diagram
galectin-3
?
show the reaction diagram
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cleaved to the 22 kDa degradation product when exposed to cells expressing membrane-anhored wild type MT1-MMP or the recombinant 50 kDa enzyme form
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?
Gelatin + H2O
?
show the reaction diagram
gelsolin + H2O
?
show the reaction diagram
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?
growth differentiation factor-1 + H2O
?
show the reaction diagram
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?
heparin-binding epidermal growth factor + H2O
?
show the reaction diagram
heparin-binding epidermal growth factor + H2O
heparin-binding epidermal growth factor mN3-fragment + ?
show the reaction diagram
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?
hepatocyte growth factor activator inhibitor-1 + H2O
?
show the reaction diagram
inactive pro-matrix metalloproteinase-2 + H2O
active matrix metalloproteinase-2 + ?
show the reaction diagram
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-
-
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?
inter-alpha inhibitor H4 + H2O
?
show the reaction diagram
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?
intercellular cell adhesion molecule-1 + H2O
?
show the reaction diagram
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?
kidney injury molecule-1 + H2O
?
show the reaction diagram
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the enzyme cleaves and sheds the substrate's ectodomain
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?
KiSS-1/metastin + H2O
?
show the reaction diagram
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?
Laminin + H2O
?
show the reaction diagram
Laminin-1 + H2O
?
show the reaction diagram
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-
-
-
?
laminin-5 + H2O
?
show the reaction diagram
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-
-
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?
laminin-5 beta3 chain + H2O
?
show the reaction diagram
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?
mannose-binding lectin + H2O
?
show the reaction diagram
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?
MCP-3/CCL7 + H2O
?
show the reaction diagram
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?
membrane-bound Semaphorin 4D + H2O
soluble Semaphorin 4D + ?
show the reaction diagram
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?
MOCAcPLGLA2pr-dinitrophenol-A-RNH2 + H2O
?
show the reaction diagram
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fluorogenic substrate
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?
MUC-1 + H2O
?
show the reaction diagram
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?
N-cadherin + H2O
?
show the reaction diagram
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-
-
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?
neuronal glial antigen 2 + H2O
?
show the reaction diagram
three (210, 160, and 51-52 kDa) major cleavage products are formed
-
-
?
Notch1 + H2O
?
show the reaction diagram
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-
-
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?
PA83
?
show the reaction diagram
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efficiently cleaved by MT1-MMP at the substrate-enzyme ratio as low as 1: 50
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?
pericentrin + H2O
?
show the reaction diagram
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?
pro-alpha v integrin + H2O
?
show the reaction diagram
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-
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?
pro-alpha5 integrin subunit + H2O
?
show the reaction diagram
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-
-
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?
pro-alpha5beta3 integrin subunit + H2O
?
show the reaction diagram
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-
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?
pro-matrix metalloproteinase-13 + H2O
?
show the reaction diagram
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activation
-
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?
pro-matrix metalloproteinase-8 + H2O
?
show the reaction diagram
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activation
-
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?
pro-MMP-2
?
show the reaction diagram
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MT1-MMP accomplishes full pro-MMP-2 activation, cleavage within the prodomain at the Asn37-Leu38 peptide bond
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?
pro-MMP-2 + H2O
?
show the reaction diagram
pro-MMP-2 + H2O
mature MMP-12 + MMP-2 pro-peptide
show the reaction diagram
pro-MMP-2 + H2O
MMP-2 + ?
show the reaction diagram
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?
pro-MMP-2 + H2O
MMP-2 + MMP-2 propeptide
show the reaction diagram
pro-MMP-2 + H2O
MMP-2 + propeptide
show the reaction diagram
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?
pro-MMP2 + H2O
MMP-2 + ?
show the reaction diagram
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activation in the presence of TIMP-2
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?
pro-tissue necrosis factor alpha + H2O
?
show the reaction diagram
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?
pro-transforming growth factor beta + H2O
?
show the reaction diagram
-
-
-
-
?
progelatinase A + H2O
?
show the reaction diagram
progelatinase A + H2O
gelatinase A + ?
show the reaction diagram
-
activation, gelatinase A is matrix metalloproteinase-2
-
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?
progelatinase A E375A + H2O
?
show the reaction diagram
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syn: pro-matrix metalloproteinase 2, cleaves at N37-L38 only
-
-
?
proMMP-13 + H2O
?
show the reaction diagram
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activation
-
-
?
proMMP-2 + H2O
?
show the reaction diagram
proMMP-2 + H2O
MMP-2 + ?
show the reaction diagram
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activation
-
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?
proMMP-8 + H2O
?
show the reaction diagram
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activation
-
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?
rat-tail tendon type I collagen + H2O
?
show the reaction diagram
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degraded by deltaTM-MT1-MMP at 37C
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?
receptor of complement component 1q + H2O
?
show the reaction diagram
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cleaves at Gly79-Gln80, cleavage with CAT/PEX domain leads to fragments with the following MW: 17 kDa, 12 kDa and 11 kDa
-
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?
receptor-activator of NF-kB ligand + H2O
?
show the reaction diagram
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-
-
-
?
recombinant mutated aggrecan fusion protein 1 + H2O
?
show the reaction diagram
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-
-
-
?
SDF-1/CXCL12 + H2O
?
show the reaction diagram
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-
-
-
?
stromal cell-derived factor 1 + H2O
?
show the reaction diagram
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-
-
-
?
syndecan + H2O
?
show the reaction diagram
-
-
-
-
?
syndecan-1 + H2O
?
show the reaction diagram
-
-
-
-
?
syndecan-1 core protein + H2O
?
show the reaction diagram
syndecan-1 G245L glutathione transferase protein + H2O
?
show the reaction diagram
-
cleaves at G82-L83 peptide bond
-
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?
testican-1 + H2O
?
show the reaction diagram
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-
-
-
?
tissue transglutaminase + H2O
?
show the reaction diagram
-
-
-
-
?
transforming growth factor-beta + H2O
?
show the reaction diagram
-
-
-
-
?
transglutaminase + H2O
?
show the reaction diagram
type 1 collagen + H2O
?
show the reaction diagram
-
-
-
-
?
Type I collagen + H2O
?
show the reaction diagram
type I collagen + H2O
denatured type I collagen
show the reaction diagram
-
bound by recombinant linker/hemopexin C domain of MT1-MMP
-
-
?
type I collagen chain alpha-1 + H2O
?
show the reaction diagram
-
-
-
-
?
type I collagen chain alpha-2 + H2O
?
show the reaction diagram
-
-
-
-
?
type II collagen + H2O
?
show the reaction diagram
-
-
-
-
?
type III collagen + H2O
?
show the reaction diagram
-
-
-
-
?
type-I collagen + H2O
?
show the reaction diagram
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-
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?
Vitronectin + H2O
?
show the reaction diagram
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-
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
CD44 + H2O
?
show the reaction diagram
-
-
-
-
?
collagen I + H2O
?
show the reaction diagram
fibroblast growth factor receptor-1 + H2O
?
show the reaction diagram
-
-
-
-
?
fibroblast growth factor receptor-4 + H2O
?
show the reaction diagram
-
-
-
-
?
Fibronectin + H2O
?
show the reaction diagram
-
-
-
-
?
growth differentiation factor-1 + H2O
?
show the reaction diagram
-
-
-
-
?
hepatocyte growth factor activator inhibitor-1 + H2O
?
show the reaction diagram
kidney injury molecule-1 + H2O
?
show the reaction diagram
-
the enzyme cleaves and sheds the substrate's ectodomain
-
-
?
Laminin + H2O
?
show the reaction diagram
Q10739
-
-
-
?
Laminin-1 + H2O
?
show the reaction diagram
-
-
-
-
?
laminin-5 + H2O
?
show the reaction diagram
-
-
-
-
?
neuronal glial antigen 2 + H2O
?
show the reaction diagram
Q10739
three (210, 160, and 51-52 kDa) major cleavage products are formed
-
-
?
Notch1 + H2O
?
show the reaction diagram
-
-
-
-
?
pro-MMP-2 + H2O
?
show the reaction diagram
-
MT-MMP1 activates MMP-2, EC 3.4.24.24
-
-
?
pro-MMP-2 + H2O
mature MMP-12 + MMP-2 pro-peptide
show the reaction diagram
-
activation of MMP-2
-
-
?
pro-MMP-2 + H2O
MMP-2 + MMP-2 propeptide
show the reaction diagram
pro-MMP-2 + H2O
MMP-2 + propeptide
show the reaction diagram
-
-
-
-
?
stromal cell-derived factor 1 + H2O
?
show the reaction diagram
-
-
-
-
?
syndecan-1 + H2O
?
show the reaction diagram
-
-
-
-
?
transforming growth factor-beta + H2O
?
show the reaction diagram
-
-
-
-
?
Type I collagen + H2O
?
show the reaction diagram
Vitronectin + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pervanadate
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-cyclopropyl-N-hydroxy-4-[(4-[4-[4-(trifluoromethyl)phenyl]piperazin-1-yl]phenyl)sulfonyl]piperidine-4-carboxamide
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4-([4-[4-(2-chlorophenyl)piperazin-1-yl]phenyl]sulfonyl)-N-hydroxytetrahydro-2H-pyran-4-carboxamide
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4-([4-[4-(2-fluorophenyl)piperazin-1-yl]phenyl]sulfonyl)-N-hydroxytetrahydro-2H-pyran-4-carboxamide
-
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4-([4-[4-(4-chlorophenyl)piperidin-1-yl]phenyl]sulfonyl)-N-hydroxytetrahydro-2H-pyran-4-carboxamide
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AB815
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against hinge region of MT1-MMP
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AG3340
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inhibits MT1-MMP in a sub-nanomolar range
AGN3340
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alpha1-PDX
-
completely abats MT1-MMP-induced gelatin degradation by A375 cells
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alpha1-PIMT1
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alpha1-proteinase inhibitor-based inhibitor by incorporating the MT1-MMP propeptide sequence into the alpha1-PI reactive-site loop, inhibits proMT1-MMP activation
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alpha1-PIPDX
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alpha1-proteinase inhibitor-based inhibitor with furin consensus cleavage sequence inserted into the reactive-site loop, inhibits proMT1-MMP activation
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anti-membrane-type 1-MMP antibody
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antibodies LEM-1 and LEM-2 inhibit endothelial cell invasion in a dose dependent manner
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batimastat
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BB-94
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CRM197
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CT1399
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inhibits endothelial cell invasion
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CT1847
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inhibits endothelial cell invasion
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decanoyl-Arg-Val-Lys-Arg-chloromethylketone
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furin inhibitor repressing activation of MMP-2
DX-2400
-
DX2400
human monoclonal antibody
-
E-64
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0.01 mM
EDTA
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10 mM, non-specific inhibitor
epigallocatechin-3-gallate
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furin
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genistein
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markedly suppresses the VEGF mRNA induction in MT clones without affecting the VEGF expression in control clones
GM6001
hemopexin
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soluble hemopexin domain inhibits collagenolysis by preventing dimerization
-
herbimycin-A
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strongly inhibits up-regulation effect of VEGF-A by MT1-MMP
ilomastat
marimastat
MT1-MMP siRNA
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collagen degrading activity is completely lost when MT1-MMP expressing cells are transfected with 100 nM MT1-MMP siRNA
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N-hydroxy-4-([4-[4-(2-hydroxyphenyl)piperidin-1-yl]phenyl]sulfonyl)tetrahydro-2H-pyran-4-carboxamide
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-
N-hydroxy-4-([4-[4-(2-methoxyphenyl)piperidin-1-yl]phenyl]sulfonyl)tetrahydro-2H-pyran-4-carboxamide
-
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N-hydroxy-4-([4-[4-(2-methylphenyl)piperazin-1-yl]phenyl]sulfonyl)tetrahydro-2H-pyran-4-carboxamide
-
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N-hydroxy-4-([4-[4-(3-methoxyphenyl)piperazin-1-yl]phenyl]sulfonyl)tetrahydro-2H-pyran-4-carboxamide
-
-
N-hydroxy-4-([4-[4-(4-methoxy-2-methylphenyl)piperidin-1-yl]phenyl]sulfonyl)tetrahydro-2H-pyran-4-carboxamide
-
-
N-hydroxy-4-([4-[4-(4-methoxyphenyl)piperazin-1-yl]phenyl]sulfonyl)tetrahydro-2H-pyran-4-carboxamide
-
-
N-hydroxy-4-([4-[4-(4-methylphenyl)piperazin-1-yl]phenyl]sulfonyl)tetrahydro-2H-pyran-4-carboxamide
-
-
N-hydroxy-4-[[4-(4-phenylpiperazin-1-yl)phenyl]sulfonyl]tetrahydro-2H-pyran-4-carboxamide
-
-
N-hydroxy-4-[[4-(4-phenylpiperidin-1-yl)phenyl]sulfonyl]tetrahydro-2H-pyran-4-carboxamide
-
-
N4-hydroxyamino-2-isobutyl-3-(thienylthiomethyl) succinyl]-L-phenylalamine-methylamide
-
-
PD98059
-
inhibits MMP-2 processing in HT1080 cells
Rac1
-
inhibits both enzyme activity and dimerization
-
Rac1(N17Rac)
-
coexpression wit MT1-MMP cDNAs leads to complete inhibition of migration
-
RECK
-
membrane anchor type proteinase inhibitor
-
reversion-inducing cysteine rich protein
-
-
-
reversion-inducing-cysteine-rich protein
-
-
-
RO28-2653
-
reduces the VEGF mRNA levels in MT clones but does not affect the basal VEGF mRNA levels in control clones
sialidase A
-
-
-
TAPI-1
-
inhibits the shedding of the MT1-MMP 18 kDa form
testican 1
-
-
-
testican 3
-
TIMP
-
-
-
TIMP 4
-
-
-
TIMP-1
-
TIMP-1 from brain is upregulated in in the infarcted tissue compared to healthy control areas, overview
-
TIMP-1 mutant forms
-
TIMP-1(T98L), TIMP-1(V4A), TIMP-1(P6V), TIMP-1(V4S), TIMP-1(P6S), TIMP-1(M66I), TIMP-1(P6A), TIMP-1(M66V), TIMP-1(M66A), TIMP-1(T2S), TIMP-1(M66L), TIMP-1(M66G), TIMP-1(V69L), TIMP-1(M66K), TIMP-1(V4A/P6V/T98L). TIMP-1 is inactive against MT1-MMP. TIMP-1 can be transformed into an active inhibitor against MT1-MMP by the mutation T98L. The resultant mutant displays inhibitory characteristics of a slow, tight binding inhibitor. The potency of the mutant can be further enhanced by the introduction of the mutations V4A and P6V
-
TIMP-2
-
TIMP-3
-
TIMP-4
-
tissue inhibitor of matrix metalloproteinase-1
-
i.e. TIMP-1, recombinant, human
-
tissue inhibitor of matrix metalloproteinases-1
-
weak inhibitor
-
tissue inhibitor of matrix metalloproteinases-2
-
effective inhibitor
-
tissue inhibitor of matrix metalloproteinases-3
-
effective inhibitor
-
tissue inhibitor of metalloproteinase 2
-
-
-
Tissue inhibitor of metalloproteinase-1
-
TIMP-1
-
Tissue inhibitor of metalloproteinase-2
-
-
-
tissue inhibitor of metalloproteinases-2
-
tissue inhibitor of MMP-2
-
tissue inhibitor of MMP-3
-
i.e. TIMP-3
-
tissue inhibitor of MMP-4
-
i.e. TIMP-4
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
claudin
-
cytokine
-
protein levels of the enzyme significantly increase by FGF-2 plus VEGF-A, only slightly by FGF-1, and not at all by VEGF-A
-
endothelin
-
-
-
furin
-
pervanadate
-
-
-
phorbol 12-myristate 13-acetate
-
-
Protein kinase C
-
-
-
TAPI-1
-
leads to higher amounts of the MT1-MMP 32 kDa form in the media, also slightly increases the amount of the 50 kDa species of MT1-MMP
TGF-beta1
-
induces MT1-MMP expression and enhances its activity
-
thyroid hormone
indirectly regulates expression of the gene
-
TIMP-2
-
required, MT-MMP1 must form a homophilic ternary complex with TIMP-2 and pro-MMP-2 to activate MMP-2
-
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00344
(7-Methoxycoumarin-4-yl)acetyl-Pro-Leu-Gly-Leu-N-3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl-Ala-Arg-NH2
-
pH 7.5, 37C, mature and mutant enzyme
0.0000000003 - 0.00000032
collagen I alpha-1 chain
-
0.00000000065 - 0.00000012
collagen I alpha-2 chain
-
0.00086 - 0.17
collagen type I alpha-1 chain
-
0.00025 - 0.53
collagen type I alpha-2 chain
-
0.009 - 0.01
MOCAcPLGLA2pr-dinitrophenol-A-RNH2
0.000034
type I collagen chain alpha-1
-
at 37C
-
0.000035
type I collagen chain alpha-2
-
at 37C
-
additional information
additional information
-
increase in substrate triple-helical thermal stability is not detrimental to enzyme binding of substrate
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.019 - 1.1
collagen I alpha-1 chain
-
1.52 - 255.6
collagen I alpha-2 chain
-
0.3 - 10.41
collagen type I alpha-1 chain
-
0.0089 - 58.61
collagen type I alpha-2 chain
-
0.02 - 0.055
MOCAcPLGLA2pr-dinitrophenol-A-RNH2
1.05
type I collagen chain alpha-1
Homo sapiens
-
at 37C
-
0.99
type I collagen chain alpha-2
Homo sapiens
-
at 37C
-
additional information
additional information
Homo sapiens
-
increase in substrate triple-helical thermal stability is detrimental to enzyme turnover of substrate
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3400000 - 880000000
collagen I alpha-1 chain
3046
-1995000000 - 2100000000
collagen I alpha-2 chain
3047
2.5 - 360
collagen type I alpha-1 chain
8948
3.5 - 350
collagen type I alpha-2 chain
8949
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0000002 - 0.000004
DX-2400
-
0.001 - 0.1
GM6001
0.000199
TIMP-1(M66A)
-
27C
-
0.000254
TIMP-1(M66G)
-
27C
-
0.000146
TIMP-1(M66I)
-
27C
-
0.000462
TIMP-1(M66K)
-
27C
-
0.000237
TIMP-1(M66L)
-
27C
-
0.000183
TIMP-1(M66V)
-
27C
-
0.000165
TIMP-1(P6A)
-
27C
-
0.000095
TIMP-1(P6S)
-
27C
-
0.000078
TIMP-1(P6V)
-
27C
-
0.00022
TIMP-1(T2S)
-
27C
-
0.0000111
TIMP-1(T98L)
-
27C
-
0.000066
TIMP-1(V4A)
-
27C
-
0.000081
TIMP-1(V4S)
-
27C
-
0.000259
TIMP-1(V69L)
-
27C
-
0.00000005 - 0.00000006
TIMP-2
-
additional information
additional information
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.01
1-cyclopropyl-N-hydroxy-4-[(4-[4-[4-(trifluoromethyl)phenyl]piperazin-1-yl]phenyl)sulfonyl]piperidine-4-carboxamide
Rattus norvegicus
-
pH not specified in the publication, temperature not speficied in the publication
0.01
4-([4-[4-(2-chlorophenyl)piperazin-1-yl]phenyl]sulfonyl)-N-hydroxytetrahydro-2H-pyran-4-carboxamide
Rattus norvegicus
-
pH not specified in the publication, temperature not speficied in the publication
0.01
4-([4-[4-(2-fluorophenyl)piperazin-1-yl]phenyl]sulfonyl)-N-hydroxytetrahydro-2H-pyran-4-carboxamide
Rattus norvegicus
-
pH not specified in the publication, temperature not speficied in the publication
0.01
4-([4-[4-(4-chlorophenyl)piperidin-1-yl]phenyl]sulfonyl)-N-hydroxytetrahydro-2H-pyran-4-carboxamide
Rattus norvegicus
-
pH not specified in the publication, temperature not speficied in the publication
0.01
N-hydroxy-4-([4-[4-(2-hydroxyphenyl)piperidin-1-yl]phenyl]sulfonyl)tetrahydro-2H-pyran-4-carboxamide
Rattus norvegicus
-
pH not specified in the publication, temperature not speficied in the publication
0.01
N-hydroxy-4-([4-[4-(2-methoxyphenyl)piperidin-1-yl]phenyl]sulfonyl)tetrahydro-2H-pyran-4-carboxamide
Rattus norvegicus
-
pH not specified in the publication, temperature not speficied in the publication
0.01
N-hydroxy-4-([4-[4-(2-methylphenyl)piperazin-1-yl]phenyl]sulfonyl)tetrahydro-2H-pyran-4-carboxamide
Rattus norvegicus
-
pH not specified in the publication, temperature not speficied in the publication
0.00286
N-hydroxy-4-([4-[4-(3-methoxyphenyl)piperazin-1-yl]phenyl]sulfonyl)tetrahydro-2H-pyran-4-carboxamide
Rattus norvegicus
-
pH not specified in the publication, temperature not speficied in the publication
0.01
N-hydroxy-4-([4-[4-(4-methoxy-2-methylphenyl)piperidin-1-yl]phenyl]sulfonyl)tetrahydro-2H-pyran-4-carboxamide
Rattus norvegicus
-
pH not specified in the publication, temperature not speficied in the publication
0.01
N-hydroxy-4-([4-[4-(4-methoxyphenyl)piperazin-1-yl]phenyl]sulfonyl)tetrahydro-2H-pyran-4-carboxamide
Rattus norvegicus
-
pH not specified in the publication, temperature not speficied in the publication
0.00822
N-hydroxy-4-([4-[4-(4-methylphenyl)piperazin-1-yl]phenyl]sulfonyl)tetrahydro-2H-pyran-4-carboxamide
Rattus norvegicus
-
pH not specified in the publication, temperature not speficied in the publication
0.01
N-hydroxy-4-[[4-(4-phenylpiperazin-1-yl)phenyl]sulfonyl]tetrahydro-2H-pyran-4-carboxamide
Rattus norvegicus
-
pH not specified in the publication, temperature not speficied in the publication
0.01
N-hydroxy-4-[[4-(4-phenylpiperidin-1-yl)phenyl]sulfonyl]tetrahydro-2H-pyran-4-carboxamide
Rattus norvegicus
-
pH not specified in the publication, temperature not speficied in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
-
assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
MMP-14 is weakly expressed in B16-F1 cells
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
MMP-8 is upregulated in the infarcted tissue compared to healthy control areas
Manually annotated by BRENDA team
-
weakly expressed
Manually annotated by BRENDA team
-
; articular
Manually annotated by BRENDA team
-
neonatal cardiac myofibroblasts
Manually annotated by BRENDA team
-
MMP-14 expression at fetomaternal interface of tubal pregnancy during gestational weeks 3-9, MMP-14 increases from distal column cytotrophoblast cells to invasive extravillous cytotrophoblast cells, also detected in villous cytotrophoblast cells, syncytiotrophoblast cells and some villous mesenchyma cells in varying abundance, distribution patterns of MMP-14 in villous cytotrophoblast cells and distal column cytotrophoblast cells in normal pregnancy is almost the same as that in tubal pregnancy
Manually annotated by BRENDA team
-
quantitative determination of content of membrane type-I MMP, TIMP-2 and MMP-2 mRNA and proteins
Manually annotated by BRENDA team
-
quantitative determination of content of membrane type-I MMP, TIMP-2 and MMP-2 mRNA and proteins
Manually annotated by BRENDA team
-
U78 glioblastoma cell line
Manually annotated by BRENDA team
-
MT1-MMP is increased in myocardial ischemia and reperfusion, myocardial, interstitial enzyme, microdialysis analysis, overview
Manually annotated by BRENDA team
MT1-MMP is upregulated during metamorphosis and coexpressed with MMP gelatinase A in connective tissue during both natural and thyroid-hormone-induced metamorphosis, MT1-MMP is also expressed in the longitudinal muscle cells of the metamorphosing intestine
Manually annotated by BRENDA team
-
furin-negative cells stably expressing wild type MT1-MMP and reconstituted furin-positive cells
Manually annotated by BRENDA team
-
prostate tumor cell line
Manually annotated by BRENDA team
-
; UACC2521; UACC2824
Manually annotated by BRENDA team
-
osteosarcoma cell line
Manually annotated by BRENDA team
-
prostate tumor cell line
Manually annotated by BRENDA team
-
expression analysis of MMP-14 in pleural mesotheliomas compared to healthy pleural specimens, overview
Manually annotated by BRENDA team
-
expression in in both the epithelial and stromal elements, low enzyme activity
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
from the oral cavity, SCC9, SCC25 and SCC68 cells
Manually annotated by BRENDA team
MT1-MMP is upregulated during metamorphosis
Manually annotated by BRENDA team
-
prostate tumor cell line
Manually annotated by BRENDA team
-
stably expresses wild type MT1-MMP
Manually annotated by BRENDA team
-
the expression level of MTI-MMP and the catalytic activitiy of the expressed protein significantly incrases 18 h after parturition, but at postpartum day 5, the mRNA expression level and catalytic activity decrease markedly
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
abnormal localisation in carcinoma cells
Manually annotated by BRENDA team
-
highest amounts
-
Manually annotated by BRENDA team
-
of immature dendritic cells. Podosomes are spot-like actin-rich structures formed at the ventral surface of monocytic and haematopoietic cells
Manually annotated by BRENDA team
additional information
-
expression analysis of MT1-MMP in cell culture
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
18000
-
immunoblot analysis of untreated cells, soluble MT1-MMP species, product of autocatalytic processing
21000
-
x * 21000, catalytic domain, SDS-PAGE
22000
-
catalytic and hinge domain
27000
-
immunoblot analysis of cells regardless of TAPI-1 treatment, contains haemopexin-like domain, formed by autocatalytic processing of the 57 kDa active form
32000
-
immunoblot analysis of untreated cells
39000
-
Western blot analysis, stable, catalytically inactive ectodomain form
42000
-
Western blot analysis, stable, catalytically inactive ectodomain form
43000
-
autolysis product, Western blot analysis
50000 - 64000
-
truncated forms, SDS-PAGE
54000
-
x * 54000, SDS-PAGE
56000
-
x * 56000, SDS-PAGE
58000
-
x * 58000, SDS-PAGE
64000
-
purified protein, SDS-PAGE
65000
-
immunoprecipitation, post-translationally modified unprocessed form, glycopeptidase F-resistant and also present if treated with inhibitors of N- and O-glycosylation
72000
-
x * 72000, mono-ubiquitinated full-length enzyme, SDS-PAGE
90000
-
MT1-GFP fusion protein, Western blot analysis
130000
-
dimeric mutant MT1EADELTATM, native PAGE
475000
-
truncated form, SDS-PAGE
570000
-
active form, SDS-PAGE
600000
-
oligomeric mutant MT1EADELTATM, native PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
-
1 * 50000, mutant MT1EADELTATM, SDS-PAGE
homodimer
-
homodimerization of MT1-MMP through its hemopexin domain is essential for cleaving type I collagen fibers at the cell surface
monomer
-
1 * 50000, mutant MT1EADELTATM, SDS-PAGE
multimer
oligomer
-
1 * 50000, mutant MT1EADELTATM, SDS-PAGE
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
-
glycosylation and palmitoylation of Cys 564 in the cytosolic tail
phosphoprotein
-
phosphorylated at Y573 and T567
proteolytic modification
ubiquitination
-
MT1-MMP is mono-ubiquitinated intracellularly at K581 within the short intracellular domain by NEDD-4. This post-translational modification is involved in MT1-MMP trafficking as well as in modulating cellular invasion through type-I collagen matrices. Ubiquitination is regulated by Src-mediated phosphorylation of MT1-MMP
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2.75 A crystal structure of the complex between the catalytic domain of human membrane type 1-matrix metalloproteinase and bovine tissue inhibitor of metalloproteinase
-
sitting drop vapor diffusion method, using 0.1 M sodium malonate pH 4.0, 20% (w/v) PEG 3350, or 4% (v/v) tacsimate pH 6.0, 12% (w/v) PEG 3350, or 0.2 M ammonium nitrate, 20% (w/v) PEG 3350 pH 6.2
-
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
high stability against autolysis and proteolysis by yeast proteases
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
18 kDa and 21 kDa fragment, homogeneity
-
affinity purification from COS-7 cells
-
catalytic domain
-
inhibitor-tethered affinity purification with BB94
-
nickel chelating column chromatography
-
purified from exclusion bodies
-
recombinant protein
-
truncated form, 90% pure
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
18 kDa inactive fragment ranging from Tyr 112 to Ala 255, 21 kDa fragment ranging from Tyr 122 to Gly 284 and truncated form lacking the cytosolic domain
-
C-terminal truncated form containing the hemopexin-like domain
-
catalytic and hinge domain
-
catalytic and hinge domains of MMP-14 (Tyr112-Ile318), containing an N-terminal methionine and C-terminal hexa-histidines (chMMP-14) expressed as inclusion body in Escherichia coli
-
catalytic domain
-
catalytic domain of MT1-MMP expressed in Escherichia coli, MT1-MMP cDNAs cloned into vector pcDNA3-zeo
-
cloned into a pcDNA3.0 expression vector
-
cloned into pSG5 vector, expression in COS-1 cells
-
cloned intop pCR-Blunt II TOPO vector
expressed in adenovirus
-
expressed in breast adenocarcinoma cells
-
expressed in COS-7 cells
-
expressed in Escherichia coli
-
expressed in Escherichia coli BL21(DE3) cells
-
expressed in Escherichia coli BL21(DE3)pLysS cells and COS-7 cells
-
expressed in lentivirus
-
expressed in LNCaP cells
-
expressed in mouse bone marrow-derived stromal cells
-
expressed in polarized human cancer cell lines A375, 451Lu, and HT-1080
-
expressed in prostate cancer LNCaP cells
-
expression analysis
-
expression in non-malignant monkey kidney epithelial BS-C-1 and CV-1 cells by co-infecting the cells with the vTF7-3 and vTF-MT1 vaccinia viruses
-
MT1-MMP cDNA subcloned between the HindIII and EcoRI sites of pCDNA3.1 Zeo+ mammalian expression vector, annealed olignucleotides coding for huMT1-MMP signal sequence cloned upstream of ECFP in the NheI-AgeI sites of the pEGFP-C1 vector, amplified residues 283-582 of huMT1-MMP cloned into the BgIII-EcoRI sites of huMT1SSc1 in-frame with EGFP
-
MT1-MMP expression in both the epithelial and stromal elements of head and neck squamous cell carcinoma cell line, low enzyme activity
-
MT1-MMP, lacking the C-terminal transmembrane and cytoplasmic domains, expression in Pichia pastoris
recombinant cdMT1-MMP expressed in Escherichia coli, recombinant deltaTM-MT1-MMP expressed in Pichia pastoris
-
recombinant expression of the truncation mutant MT1EADELTATM in Escherichia coli, expression of the PEX-domain-deleted MT1-MMP mutant
-
stable expression of FLAG-tagged MT1-MMP in A-431 cells, co-expression with Myc-tagged MT1-MMP
-
the catalytic domain (Tyr112-Val335) is expressed in Escherichia coli BL21 cells
-
truncated forms, mutations and wild type
-
two truncated forms: CAT domain and CAT/PEX domain
-
wild-type and various mutants: deletion of catalytic domain, deletion of POX domain, deletion of cytoplasmic tail, deletion of 8, 8 or 12 amino acids at C-terminus, all deletions except catalytic and PEX domain reduced internalization of the protein
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
cyclosporine A inhibits expression of membrane-type I MMP in gingiva
-
cyclosporine A inhibits expression of membrane-type I MMP, but not of TIMP-2, in gingiva. Transcription of MMP-2 is unaffected, but translation is inhibited
-
in patients with tuberculosis, induced sputum enzyme mRNA levels are increased 5.1fold compared with matched controls. Mycobacterium tuberculosis infection of primary human monocytes increases enzyme surface expression 31.7fold and gene expression 24.5fold
-
interleukin-6 enhances matrix metalloproteinase-14 expression through activator protein-1, AP-1, and via the induced RAF-mitogen-activated protein kinase kinase-extracellular signal-regulated kinase 1/2-activator protein-1 pathway, overview
-
MMP-8 is upregulated after stroke in brain in the infarcted tissue compared to healthy control areas, overview
-
Snail increases the expression of membrane type 1-matrix metalloproteinase through activation of ERK-MAPK signaling
-
the enzyme is induced by collagen-gel culture or con-canavalin A treatment
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C574A
-
inefficient in stimulating cell adhesion, migration and invasion, mutation negatively affects cell adhesion
C574S
-
substitution in the cytoplasmic domain, reduction of pro-MMP2 activation, no up-regulation of VEGF expression
K110A
-
processing of the enzyme is blocked
K44A
-
dominant negative dynamin mutation controlled by a separate cytomegalovirus promoter MT1/K44A, leading to increased substrate digestion that is contributed by enhanced cell migration resulting from the accumulation of MT1-MMP ant the plasma membrane
K581R
-
ubiquitination-deficient mutant
L571A/L572A
-
mutation leads to reduced internalization of enzyme
L571A/L572A/L578A/L579A
-
mutation leads to reduced internalization of enzyme
L571A/L572A/Y573A
-
mutation leads to reduced internalization of enzyme, no effect on cell motility
L578A/L579A
-
mutation leads to reduced internalization of enzyme
MT1F-DELTACat
-
catalytic domain-deletion mutant
R108A
-
processing of the enzyme is blocked
R111A
-
processing of the enzyme is blocked
R89A
-
can activate matrix metalloproteinase 2
T567A
-
substitution in the cytoplasmic domain, pro-MMP2-activating capacity not affected, similar VEGF upregulation
V582A
-
internalization of enzyme is not affected
Y112F
-
normal enzyme processing
Y573A/L571A/L572A/L578A/L579A
-
mutation leads to reduced internalization of enzyme
E240A
-
catalytically inactive
additional information
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
dialysis against a 10fold volume of 50 mM Tris-HCl pH 8.5, 100 mM NaCl, 10 mM CaCl2, 10 mM zinc acetate, and 2 M urea
-
refolding of the purified polypeptide to active enzyme by gradient dialysis with urea gradient from 6 M decreasing to 0 M and 2-mercaptoethanol gradient from 150 mM decreasing to 0 mM in the presence of CaCl2 and ZnCl2
-