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Information on EC 3.4.24.24 - gelatinase A and Organism(s) Homo sapiens and UniProt Accession P08253

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     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.24 Metalloendopeptidases
                3.4.24.24 gelatinase A
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Select one or more organisms in this record:
This record set is specific for:
Homo sapiens
UNIPROT: P08253 not found.
Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Synonyms
mmp-2, matrix metalloproteinase-2, matrix metalloproteinase 2, type iv collagenase, metalloproteinase-2, collagenase iv, mmp 2, collagenase type iv, 72-kda gelatinase, matrix metalloprotease 2, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
72 kDa Gelatinase
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72 kDa Gelatinase type A
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72 kDa type IV collagenase
247
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72-kDa Gelatinase
Collagenase IV
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Collagenase type IV
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human gelatinase A
247
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human matrix metalloproteinase 2
247
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human matrix metalloproteinase-2
247
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matrix metallopeptidase 2
283382
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matrix metalloprotease 2
247
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Matrix metalloproteinase 2
matrix metalloproteinase-2
matrix metalloprotenase-2
247
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metalloproteinase-2
247
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metrix metalloproteinase-2
247
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MMP 2
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MMP-2
MMP2
247
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Type IV collagen metalloproteinase
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Type IV collagenase
Type IV collagenase/gelatinase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
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CAS REGISTRY NUMBER
COMMENTARY hide
146480-35-5
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(7-methoxycoumarin-4-yl)acetyl-Pro-Leu-Gly-Leu-DPA-Ala-Arg-NH2 + H2O
(7-methoxycoumarin-4-yl)acetyl-Pro-Leu-Gly + Leu-DPA-Ala-Arg-NH2
show the reaction diagram
-
-
-
-
?
fibrillin-1 + H2O
?
show the reaction diagram
-
from eye oxytalan fibers, degradation in vitro
-
-
?
fibrillin-2 + H2O
?
show the reaction diagram
-
from eye oxytalan fibers, degradation in vitro
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-
?
Gelatin + H2O
?
show the reaction diagram
Type IV collagen + H2O
?
show the reaction diagram
(7-methoxycoumarin-4-yl)acetyl-L-Pro-Leu-Gly-Leu-Dap-Ala-Arg-NH2 + H2O
?
show the reaction diagram
-
a quenched fluorogenic substrate
-
-
?
(7-methoxycoumarin-4-yl)acetyl-Pro-Leu-Gly-Leu-2,6-diaminopimelyl-Ala-Arg-NH2 + H2O
?
show the reaction diagram
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-
-
-
?
(7-methoxycoumarin-4-yl)acetyl-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly-Leu-Lys(2,4-dinitrophenyl)-Gly + H2O
?
show the reaction diagram
-
a short 11-amino-acid collagen-like peptide substrate, NFF-1, cleavage of NFF-1 by MMP-2 does not require CBD-mediated substrate binding for degradation to occur
-
-
?
110000 MW cell-surface amyloid protein precursor + H2O
?
show the reaction diagram
-
amyloid protein precursor of Alzheimer's disease, cleavage to a 1000 MW form of the protein
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2,4-Dinitrophenyl-Pro-Leu-Gly-Leu-Trp-Ala-D-Ala-NH2 + H2O
?
show the reaction diagram
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-
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7-methylcoumaryl-L-Pro-L-Lys-L-Gln-L-Gln-L-Phe-L-Phe-Gly-L-Leu-L-Lys-(2,4-dinitrophenyl)-Gly + H2O
?
show the reaction diagram
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-
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?
Ac-Pro-Leu-Gly-[2-mercapto-4-methylpentanoyl]-Leu-Gly-OEt + H2O
?
show the reaction diagram
-
-
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?
Acetyl-Pro-Leu-Gly-thioester-Leu-Leu-Gly ethyl ester + H2O
?
show the reaction diagram
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alpha1(V)436-447 fTHP + H2O
?
show the reaction diagram
-
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-
?
Azocoll + H2O
?
show the reaction diagram
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Bovine fibrinogen + H2O
?
show the reaction diagram
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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
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?
Cartilage proteoglycan + H2O
?
show the reaction diagram
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Collagen + H2O
?
show the reaction diagram
collagen type IV + H2O
?
show the reaction diagram
collagene type IV + H2O
?
show the reaction diagram
Dnp-Pro-beta-cyclohexyl-Ala-Gly-Cys(Me)-His-Ala-Lys(N-Me-Abz)-NH2 + H2O
?
show the reaction diagram
-
-
-
?
Elastin + H2O
?
show the reaction diagram
ephB1 + H2O
?
show the reaction diagram
extracellular matrix components + H2O
?
show the reaction diagram
-
-
-
?
Fibrinogen + H2O
?
show the reaction diagram
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?
Fibronectin + H2O
?
show the reaction diagram
fTHP-3 + H2O
?
show the reaction diagram
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-
?
Galectin-3 + H2O
?
show the reaction diagram
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a galactoside-binding protein, major cleavage site: Ala62-Tyr63
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Gelatin + H2O
?
show the reaction diagram
Gly-Pro-Gln-Gly-Ile-Ala-Gly-Gln + H2O
Gly-Pro-Gln-Gly + Ile-Ala-Gly-Gln
show the reaction diagram
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Gly-Pro-Gln-Gly-Ile-Ala-Ser-Gln + H2O
Gly-Pro-Gln-Gly + Ile-Ala-Ser-Gln
show the reaction diagram
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Gly-Pro-Gln-Gly-Ile-Phe-Gly-Gln + H2O
Gly-Pro-Gln-Gly + Ile-Phe-Gly-Gln
show the reaction diagram
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Gly-Pro-Gln-Gly-Ile-Trp-Gly-Gln + H2O
Gly-Pro-Gln-Gly + Ile-Trp-Gly-Gln
show the reaction diagram
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Laminin + H2O
?
show the reaction diagram
LS276-THP + H2O
?
show the reaction diagram
-
development and evaluation of an activatable NIR fluorescent probe LS276-THP for in vivo detection of cancer-related matrix metalloproteinase activity based on a triplehelical peptide substrate with high specificity for MMP-2 and MMP-9 relative to other members of the MMP family, overview. Triple-helical peptides are suitable for highly specific in vivo detection of tumor-related MMP-2 and MMP-9 activity
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?
Mca-Pro-Leu-Gly-Leu-Dap(Dnp)-Ala-Arg-NH2 + H2O
?
show the reaction diagram
-
quenched fluorescent peptide
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?
Mca-Pro-Leu-Gly-Leu-Dap-Ala-Arg-NH2 + H2O
?
show the reaction diagram
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?
Mca-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2 + H2O
?
show the reaction diagram
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MOAcPLGLA2pr(Dnp)-AR-NH2 + H2O
?
show the reaction diagram
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fluorogenic quenching substrate
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?
Neonatal human proteoglycan + H2O
?
show the reaction diagram
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cleavage of the His16-Ile17 bond and the Leu25-Leu26 bond
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peptide A13 + H2O
?
show the reaction diagram
peptide A13P + H2O
?
show the reaction diagram
-
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?
peptide A13R + H2O
?
show the reaction diagram
peptide A21 + H2O
?
show the reaction diagram
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?
peptide A21A + H2O
?
show the reaction diagram
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?
peptide A3 + H2O
?
show the reaction diagram
peptide A34 + H2O
?
show the reaction diagram
peptide B37 + H2O
?
show the reaction diagram
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?
peptide B49 + H2O
?
show the reaction diagram
-
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?
peptide B74 + H2O
?
show the reaction diagram
peptide B74P + H2O
?
show the reaction diagram
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?
peptide B74R + H2O
?
show the reaction diagram
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?
peptide C15 + H2O
?
show the reaction diagram
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non-selective peptide substrate
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?
peptide C9 + H2O
?
show the reaction diagram
peptide C9R + H2O
?
show the reaction diagram
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?
peptide m1A11 + H2O
?
show the reaction diagram
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non-selective peptide substrate
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?
peroxynitrite-treated fibrinogen + H2O
?
show the reaction diagram
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?
Progelatinase B + H2O
?
show the reaction diagram
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activation to an 82000 MW active form
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Type I collagen + H2O
?
show the reaction diagram
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?
Type IV collagen + H2O
?
show the reaction diagram
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?
type V collagen + H2O
?
show the reaction diagram
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?
Vitronectin + H2O
?
show the reaction diagram
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a 65000 MW and a 75000 MW form
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additional information
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
Gelatin + H2O
?
show the reaction diagram
Type IV collagen + H2O
?
show the reaction diagram
Collagen + H2O
?
show the reaction diagram
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?
collagen type IV + H2O
?
show the reaction diagram
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?
collagene type IV + H2O
?
show the reaction diagram
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?
extracellular matrix components + H2O
?
show the reaction diagram
-
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?
Fibrinogen + H2O
?
show the reaction diagram
-
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?
Gelatin + H2O
?
show the reaction diagram
-
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?
additional information
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
NaCl
-
4-bladed beta-propeller protein in which the 4 blades are arranged around a channel-like opening in which Ca2+ and a Na+Cl- ion pair are bound
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
APP-IP-TIMP-2
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inhibition evaluation and kinetics, mechanism in concanavalin A-stimulated HT1080 fibrosarcoma cells, expression of APP-IP-TIMP-2 in HT1080 cells, overview. The ten amino acid residue sequence of APP-derived MMP-2 selective inhibitory peptide (APP-IP) is added to the N-terminus of tissue inhibitors of metalloproteinase 2, TIMP-2. The APP-IP and TIMP-2 regions of the fusion protein are designed to interact with the active site and the hemopexin-like domain of MMP-2, respectively.The reactive site of the TIMP-2 region, which has broad specificity against MMPs, is blocked by the APP-IP adduct. The recombinant APP-IP-TIMP-2 shows strong inhibitory activity toward MMP-2 whereas its inhibitory activity toward MMP-1, MMP-3, MMP-7, MMP-8, MMP-9, or MT1--MMP is six orders of magnitude or more weaker. Compared with the decapeptide APP-IP, APP-IP-TIMP-2 shows a much longer half-life in cultured tumor cells
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N-(R)-(2-(hydroxyaminocarbonyl)methyl)-4-methylpentanoyl-L-naphthylalanyl-L-alanine-2-aminoethyl amide
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TAPI-1
tissue inhibitors of metalloproteinase 2
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TIMP2
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(2E)-3-(N-hydroxycarbamoyl)-2-(3-phenylpropylidene)propionyl-L-tryptophan-N-methylamide
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(2E)-3-(N-hydroxycarbamoyl)-2-heptylidenepropionyl-L-tryptophan-N-methylamide
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(2E)-3-(N-hydroxycarbamoyl)-2-isopropionyl-L-tryptophan-N-methylamide
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(2E)-3-(N-hydroxycarbamoyl)-2-[(2E)-3-phenylprop-2-en-1-ylidene]propionyl-L-tryptophan-N-methylamide
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(2E)-3-(N-hydroxycarbamoyl)-2-[(2E)-but-2-en-1-ylidene]propionyl-L-tryptophan-N-methylamide
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(2R)-2-[(4-biphenylylcarbonyl)amino]-N-hydroxy-3-(1H-indol-3-yl)propionamide
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(2R)-2-[(4-biphenylylsulfonyl)amino]-3-phenylpropionic acid
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(2R)-2-[(4-biphenylylsulfonyl)amino]-3-phenylpropionic acid benzyl ester
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(2R)-2-[[4-[benzenesulfonylhydrazonomethyl]benzenesulfonyl]-amino]-3-(1H-indol-3-yl)propionic acid methyl ester
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(2R)-2-[[4-[benzenesulfonylhydrazonomethyl]benzenesulfonyl]-amino]-3-methylbutanoic acid tert-butyl ester
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(2R)-2-[[5-(4-methoxyphenyl)thiophene-2-sulfonyl]-amino]-3-methylbutanoic acid
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(2R)-2-[[5-(4-methoxyphenyl)thiophene-2-sulfonyl]-amino]-3-methylbutanoic acid methyl ester
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(2R)-3-(1H-indol-3yl)-2-[[4-(phenylazo)benzenesulfonyl]amino]propionic acid
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(2R)-3-(1H-indol-3yl)-2-[[4-[phenylaminocarbonyl]-benzenesulfonyl]amino]propionic acid benzyl ester
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(2R)-3-methyl-2-[4-[phenoxybenzenesulfonyl]amino]butanoic acid
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(2R)-3-methyl-2-[[4-[(4-nitrobenzoyl)-amino]benzenesulfonyl]amino]butanoic acid
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(2R)-3-methyl-2-[[4-[(4-nitrobenzoyl)amino]benzenesulfonyl]amino]butanoic acid tert-butyl ester
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(2R)-3-methyl-2-[[4-[2-[4-methylmercaptophenyl]-2H-tetrazol-5-yl]benzenesulfonyl]-amino]butanoic acid
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(2R)-3-methyl-2-[[4-[2-[methylmercaptophenyl]-2H-tetrazol-5-yl]benzenesulfonyl]-amino]butanoic acid tert-butyl ester
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(2R)-3-methyl-2-[[5-[(4-methylphenyl)ethynyl]thiophene-2-sulfonyl]-amino]butanoic acid methyl ester
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(2R)-N-(benzyloxy)-2-[(4-biphenylsulfonyl)amino]-3-phenylpropionamide
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(2R)-N-hydroxy-3-methyl-2-[(4-phenoxybenzenesulfonyl)amino]butanamide
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(2R)-[(4-biphenylsulfonyl)amino]-N-hydroxy-3-phenylpropionamide
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(4-phenoxyphenylsulfonyl)methylthiirane
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selective inhibitor of MMP2
1,10-phenanthroline
1,4-dithiothreitol
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2-(4-(4-[(2-thiiranylpropyl)sulfonyl]phenoxy)phenyl)acetic acid
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selective inhibitor
2-([4-[3'-(2-aminoethoxy)-2-methylbiphenyl-4-yl]piperidin-1-yl]sulfonyl)-N-hydroxy-2-methylpropanamide
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2-[(4-biphenyl-4-yl-3,6-dihydropyridin-1(2H)-yl)sulfonyl]-N-hydroxyacetamide
-
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2-[(4-[3'-[2-(dimethylamino)ethoxy]-2-methylbiphenyl-4-yl]piperidin-1-yl)sulfonyl]-N-hydroxy-2-methylpropanamide
-
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2-[(biphenyl-4-ylsulfonyl)(isobutyl)amino]-N-hydroxyacetamide
-
50% inhibition at 13 nM, comparison with inhibitory effect on matrix metalloproteinases MMP-3, MMp-7, MMP-9
2-[(biphenyl-4-ylsulfonyl)(isopropoxy)amino]-N-hydroxyacetamide
-
50% inhibition at 12 nM, comparison with inhibitory effect on matrix metalloproteinases MMP-3, MMp-7, MMP-9
2-[[4-(2,3'-dimethylbiphenyl-4-yl)-3,6-dihydropyridin-1(2H)-yl]sulfonyl]-N-hydroxyacetamide
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2-[[4-(2-chlorobiphenyl-4-yl)-3,6-dihydropyridin-1(2H)-yl]sulfonyl]-N-hydroxyacetamide
-
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2-[[4-(2-ethylbiphenyl-4-yl)-3,6-dihydropyridin-1(2H)-yl]sulfonyl]-N-hydroxyacetamide
-
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2-[[4-(2-fluorobiphenyl-4-yl)-3,6-dihydropyridin-1(2H)-yl]sulfonyl]-N-hydroxyacetamide
-
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2-[[4-(3'-ethoxy-2-methylbiphenyl-4-yl)-3,6-dihydropyridin-1(2H)-yl]sulfonyl]-N-hydroxyacetamide
-
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2-[[4-(3'-ethoxy-2-methylbiphenyl-4-yl)piperidin-1-yl]sulfonyl]-N-hydroxy-2-methylpropanamide
-
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2-[[4-(3'-ethyl-2-methylbiphenyl-4-yl)-3,6-dihydropyridin-1(2H)-yl]sulfonyl]-N-hydroxyacetamide
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4-(2-phenyl-2H-tetrazol-5-yl)benzenesulfonyl chloride
-
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4-(3-phenylureido) benzenesulfonyl chloride
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4-(4-phenoxphenylsulfonyl)butane-1,2-dithiol
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4-Aminobenzoyl-Gly-Pro-D-Leu-D-Ala-NHOH
-
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5-(4-phenoxphenylsulfonyl)pentane-1,2-dithiol
-
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advanced glycation products
-
inhibit the enzyme mediated through upregulation of the advanced glycation product receptor, overview
-
Ag-3340
-
i.e. N-hydroxy-2,2-dimethyl-4-[(4-phenoxyphenyl)sulfonyl]thiomorpholine-3-carboxamide, 50% inhibition at 0.083 nM, comparison with inhibitory effect on matrix metalloproteinases MMP-3, MMp-7, MMP-9
batimastat
-
i.e. BB-94, a peptidomimetic inhibitor
benzyloxycarbonyl-L-Trp-OH
-
-
beta-amyloid precursor protein
-
APP
CGS27023A
-
50% inhibition at 20 nM, comparison with inhibitory effect on matrix metalloproteinases MMP-3, MMp-7, MMP-9
chitooligosaccharides
-
inhibit MMP-2 enzyme expression, decrease of the gene expression and transcriptional activity of MMP-2, and catalytic activity in primary dermal fibroblasts, chitooligosaccharides of 3-5 kDa are most effective
D-tryptophan benzyl ester trifluoroacetate
-
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D-tryptophan methyl ester tosylate
-
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dibenzofuran-2-sulfonyl chloride
-
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dimethyl sulfoxide
-
presence of 2% dimethyl sulfoxide disrupts interactions of enzyme with substrate and thereby reduces activity by 70%
endostatin
-
-
-
extracellular domain of beta-amyloid peptide
-
the extracellular domain of beta-amyloid precursor protein contains an inhibitor against MMP-2, the inhibitor is localized within the ISYGNDALMP sequence of APP, overview
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galardin
-
-
glycine
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-
GNDAMPL
-
APP-IP delta N3
GSSG
-
-
ilomastat
ISYGADALMP
-
APP-IP delta N/A
ISYGNAALMP
-
APP-IP delta D/A
ISYGNDAAMP
-
APP-IP delta L/A
ISYGNDAL
-
APP-IP delta C2
ISYGNDALM
-
APP-IP delta C1
ISYGNDALMP
ISYGNDALMPSL
-
APP586-597
ISYGNDALMPSLTETK
-
APP586-601
L-ascorbic acid
-
-
L-cysteine
-
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L-histidine
-
-
L-homocysteine
-
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L-methionine
-
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methyl 2-(4-(4-[(2-thiiranylpropyl)-sulfonyl]phenoxy)phenyl)acetate
-
mechanism-based inhibitor, selective for enzyme
N-acetylcysteine
-
-
N-hydroxy-2-(isobutyl[(4-methoxyphenyl)sulfonyl]amino)acetamide
-
50% inhibition at 6.9 nM, comparison with inhibitory effect on matrix metalloproteinases MMP-3, MMp-7, MMP-9
N-hydroxy-2-([4-[2-(trifluoromethyl)biphenyl-4-yl]-3,6-dihydropyridin-1(2H)-yl]sulfonyl)acetamide
-
-
N-hydroxy-2-([4-[2-methyl-3'-(trifluoromethoxy)biphenyl-4-yl]-3,6-dihydropyridin-1(2H)-yl]sulfonyl)acetamide
-
-
N-hydroxy-2-([4-[3'-(2-hydroxyethoxy)-2-methylbiphenyl-4-yl]piperidin-1-yl]sulfonyl)-2-methylpropanamide
-
-
N-hydroxy-2-([4-[3'-(2-methoxyethoxy)-2-methylbiphenyl-4-yl]piperidin-1-yl]sulfonyl)-2-methylpropanamide
-
-
N-hydroxy-2-([4-[3'-(methoxymethyl)-2-methylbiphenyl-4-yl]-3,6-dihydropyridin-1(2H)-yl]sulfonyl)acetamide
-
-
N-hydroxy-2-methyl-2-[(4-[2-methyl-3'-[2-(methylamino)ethoxy]biphenyl-4-yl]piperidin-1-yl)sulfonyl]propanamide
-
-
N-hydroxy-2-[(4-[4-[6-(2-hydroxyethoxy)pyridin-2-yl]-3-methylphenyl]piperidin-1-yl)sulfonyl]-2-methylpropanamide
-
-
N-hydroxy-2-[[4-(2-methylbiphenyl-4-yl)-3,6-dihydropyridin-1(2H)-yl]sulfonyl]acetamide
-
-
N-hydroxy-2-[[4-(3'-methoxy-2-methylbiphenyl-4-yl)-3,6-dihydropyridin-1(2H)-yl]sulfonyl]acetamide
-
-
NaCl
-
binding to heparin and fibronectin can be disrupted by 0.3 M NaCl
peptide P713
-
inhibits the binding of the CBD as well as MMP-2E404A to gelatin, no inhibition of MMP-2 lacking thr CBD domain, competitively, P713 inhibits MMP-2 activities by blocking substrate access to the CBD exodomain, mechanism, overview
-
procyanidin oligomers
-
from Japanese quince, Chaenomeles japonica, fruit inhibit activity of MMP-2
-
SB-3CT
-
mechanism-based synthetic inhibitor
SC-74020
-
hydroxamic acid inhibitor
Stromelysin catalytic domain inhibitors
-
gelatinase A synthetic 19000 MW catalytic domain
-
SYGNDAMPL
-
APP-IP delta N1
ter-butyloxycarbonyl-L-Trp-OH
-
-
TIMP
-
-
-
TIMP-1
-
-
-
TIMP-2
-
TIMP-4
-
tissue inhibitor of metalloproteinases
-
Tissue inhibitor of metalloproteinase-1
-
-
-
Tissue inhibitor of metalloproteinase-2
-
Tissue inhibitor of metalloproteinases
-
-
-
tissue inhibitor of metalloproteinases-2
-
TIMP-2, complex formation with MMP-14 and MMP-2 activates the enzyme, overview
-
UK-370106
-
-
YGNDAMPL
-
APP-IP delta N2
Zn2+
-
required, synthetic 19000 MW catalytic domain, inhibition at high concentration
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4-aminophenylmercuric acetate
-
-
aminophenylmercuric acetate
-
-
heparan sulfate
-
essential for thrombin-mediated activation of pro-MMP-2
membrane-type 1 matrix metalloproteinase
-
activity in the extracellular environment is modulated by this activator
-
MMP-14
-
MMP-14 activates MMP-2 during degeneration of invertebral disc, a major activation pathway of MMP-2 involves complex formation with MMP-14 and a tissue inhibitor of metalloproteinases-2, TIMP-2, overview
-
p-aminophenyl-mercuric acetate
-
-
syndecan-1
-
expression of syndecan-1 increases thrombin-mediated activation of pro-MMP-2 in K562 cells
-
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
-
additional information
-