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

BRENDA support

BRENDA Home
show all | hide all No of entries

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

for references in articles please use BRENDA:EC3.4.24.24
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.24 Metalloendopeptidases
                3.4.24.24 gelatinase A
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Homo sapiens
UNIPROT: P08253 not found.
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Synonyms
mmp-2, gelatinase, matrix metalloproteinase-2, matrix metalloproteinase 2, gelatinase a, type iv collagenase, metalloproteinase-2, progelatinase, collagenase iv, mmp 2, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
human matrix metalloproteinase-2
-
matrix metallopeptidase 2
-
Matrix metalloproteinase 2
-
metrix metalloproteinase-2
-
progelatinase
-
Type IV collagenase
-
72 kDa Gelatinase
-
-
-
-
72 kDa Gelatinase type A
-
-
-
-
72 kDa type IV collagenase
-
-
72-kDa Gelatinase
Collagenase IV
-
-
-
-
Collagenase type IV
-
-
-
-
human gelatinase A
-
-
human matrix metalloproteinase 2
-
-
human matrix metalloproteinase-2
-
-
matrix metalloprotease 2
-
-
Matrix metalloproteinase 2
matrix metalloprotenase-2
-
-
metalloproteinase-2
-
-
MMP 2
-
-
-
-
MMP2
-
-
Type IV collagen metalloproteinase
-
-
-
-
Type IV collagenase
Type IV collagenase/gelatinase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
146480-35-5
-
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
-
-
-
?
Collagen + H2O
?
show the reaction diagram
-
-
-
?
ephB1 + H2O
?
show the reaction diagram
-
-
?
extracellular matrix components + H2O
?
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
-
-
?
Gelatin + H2O
?
show the reaction diagram
Mca-KPLGL-(Dpa)-AR-NH2 + H2O
?
show the reaction diagram
-
-
-
?
peptide A13 + H2O
?
show the reaction diagram
-
-
?
peptide A13R + H2O
?
show the reaction diagram
-
-
?
peptide A3 + H2O
?
show the reaction diagram
-
-
?
peptide A34 + H2O
?
show the reaction diagram
-
-
?
peptide B74 + H2O
?
show the reaction diagram
-
-
?
peptide C15 + H2O
?
show the reaction diagram
non-selective peptide substrate
-
?
peptide C9 + H2O
?
show the reaction diagram
-
-
?
peptide m1A11 + H2O
?
show the reaction diagram
non-selective peptide substrate
-
?
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
-
-
-
-
?
(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
-
-
?
2,4-Dinitrophenyl-Pro-Leu-Gly-Leu-Trp-Ala-D-Ala-NH2 + H2O
?
show the reaction diagram
-
-
-
-
?
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
-
-
-
-
?
Ac-Pro-Leu-Gly-[2-mercapto-4-methylpentanoyl]-Leu-Gly-OEt + H2O
?
show the reaction diagram
-
-
-
?
Acetyl-Pro-Leu-Gly-thioester-Leu-Leu-Gly ethyl ester + H2O
?
show the reaction diagram
-
-
-
-
?
alpha1(V)436-447 fTHP + H2O
?
show the reaction diagram
-
-
-
?
Azocoll + H2O
?
show the reaction diagram
-
-
-
-
?
Bovine fibrinogen + H2O
?
show the reaction diagram
-
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
-
-
?
Cartilage proteoglycan + H2O
?
show the reaction diagram
-
-
-
-
?
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
-
-
-
?
Fibrinogen + H2O
?
show the reaction diagram
-
-
-
-
?
Fibronectin + H2O
?
show the reaction diagram
fTHP-3 + H2O
?
show the reaction diagram
-
-
-
?
Galectin-3 + H2O
?
show the reaction diagram
-
a galactoside-binding protein, major cleavage site: Ala62-Tyr63
-
-
?
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
-
-
-
?
Gly-Pro-Gln-Gly-Ile-Ala-Ser-Gln + H2O
Gly-Pro-Gln-Gly + Ile-Ala-Ser-Gln
show the reaction diagram
-
-
-
?
Gly-Pro-Gln-Gly-Ile-Phe-Gly-Gln + H2O
Gly-Pro-Gln-Gly + Ile-Phe-Gly-Gln
show the reaction diagram
-
-
-
?
Gly-Pro-Gln-Gly-Ile-Trp-Gly-Gln + H2O
Gly-Pro-Gln-Gly + Ile-Trp-Gly-Gln
show the reaction diagram
-
-
-
?
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
-
-
?
Mca-Pro-Leu-Gly-Leu-Dap(Dnp)-Ala-Arg-NH2 + H2O
?
show the reaction diagram
-
quenched fluorescent peptide
-
?
Mca-Pro-Leu-Gly-Leu-Dap-Ala-Arg-NH2 + H2O
?
show the reaction diagram
-
-
-
?
Mca-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2 + H2O
?
show the reaction diagram
-
-
-
-
?
MOAcPLGLA2pr(Dnp)-AR-NH2 + H2O
?
show the reaction diagram
-
fluorogenic quenching substrate
-
?
Neonatal human proteoglycan + H2O
?
show the reaction diagram
-
cleavage of the His16-Ile17 bond and the Leu25-Leu26 bond
-
-
?
peptide A13 + H2O
?
show the reaction diagram
-
-
-
?
peptide A13P + H2O
?
show the reaction diagram
-
-
-
?
peptide A13R + H2O
?
show the reaction diagram
-
-
-
?
peptide A21 + H2O
?
show the reaction diagram
-
-
-
?
peptide A21A + H2O
?
show the reaction diagram
-
-
-
?
peptide A3 + H2O
?
show the reaction diagram
-
-
-
?
peptide A34 + H2O
?
show the reaction diagram
-
-
-
?
peptide B37 + H2O
?
show the reaction diagram
-
-
-
?
peptide B49 + H2O
?
show the reaction diagram
-
-
-
?
peptide B74 + H2O
?
show the reaction diagram
-
-
-
?
peptide B74P + H2O
?
show the reaction diagram
-
-
-
?
peptide B74R + H2O
?
show the reaction diagram
-
-
-
?
peptide C9 + H2O
?
show the reaction diagram
-
-
-
?
peptide C9R + H2O
?
show the reaction diagram
-
-
-
?
peroxynitrite-treated fibrinogen + H2O
?
show the reaction diagram
-
-
-
-
?
Progelatinase B + H2O
?
show the reaction diagram
-
activation to an 82000 MW active form
-
-
?
Type I collagen + H2O
?
show the reaction diagram
-
-
-
?
Type IV collagen + H2O
?
show the reaction diagram
-
-
-
?
type V collagen + H2O
?
show the reaction diagram
-
-
-
?
Vitronectin + H2O
?
show the reaction diagram
-
a 65000 MW and a 75000 MW form
-
-
?
vitronectin of MW 65000 + H2O
?
show the reaction diagram
-
-
-
-
?
vitronectin of MW 65000 and 75000 + H2O
?
show the reaction diagram
-
-
-
-
?
vitronectin of MW 75000 + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
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
Collagen + H2O
?
show the reaction diagram
-
-
-
?
extracellular matrix components + H2O
?
show the reaction diagram
-
-
?
Gelatin + H2O
?
show the reaction diagram
Type IV collagen + H2O
?
show the reaction diagram
Collagen + H2O
?
show the reaction diagram
-
-
-
-
?
collagen type IV + H2O
?
show the reaction diagram
-
-
-
-
?
collagene type IV + H2O
?
show the reaction diagram
-
-
-
-
?
Fibrinogen + H2O
?
show the reaction diagram
-
-
-
-
?
Gelatin + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
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
4-(4-phenoxphenylsulfonyl)butane-1,2-dithiol
-
5-(4-phenoxphenylsulfonyl)pentane-1,2-dithiol
-
alpha-linolenic acid
-
alpha2-Macroglobulin
-
-
APP-IP-TIMP-2
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
-
docosahexaenoic acid
-
gamma-linolenic acid
-
isovitexin
interacts with enzyme residues Glu121, Leu83, Ala84, Pro140, Ile141, His120, Ala136, Leu116, Ala139, and Leu137, binding structure analysis, and modelling, overview
linoleic acid
-
N-(R)-(2-(hydroxyaminocarbonyl)methyl)-4-methylpentanoyl-L-naphthylalanyl-L-alanine-2-aminoethyl amide
TAPI-1
N-isobutyl-N-(4-methoxyphenylsulfonyl)glycyl hydroxamic acid
NNGH
oleic acid
-
procollagen C-terminal proteinase enhancer
PCPE
-
RECK
reversion-inducing cysteine-rich protein with Kazal motifs
-
SB-3CT
mechanism-based synthetic inhibitor
TIMP-1
binding also involves interaction between TIMP and the MMP-2 Hpx-like domain
-
TIMP-3
binding also involves interaction between TIMP and the MMP-2 Hpx-like domain
-
TIMP-4
binding also involves interaction between TIMP and the MMP-2 Hpx-like domain
-
tissue factor pathway inhibitor
TFPI-2
-
tissue inhibitor of metalloproteinases-2
TIMP-2, a physiological inhibitor of MMPs. proMMP-2 can be secreted either in a free form or already complexed with TIMP-2 through its C-terminal domain. In the first case, a TIMP-2 that inhibits a cell membrane-anchored MT1-MMP by interaction between its N-terminal inhibitory domain and the catalytic domain of MT1-MMP, acts as a binding site for free proMMP-2 by interaction between the proMMP-2 Hpx-like domain and the TIMP-2 C-terminal domain. ProMMP-2 present in the resulting MT1-MMP-TIMP-2-proMMP-2 complex can then be activated by another adjacent TIMP-2-free MT1-MMP. In the second case, the N-terminal inhibitory domain of TIMP-2 in the proMMP-2-TIMP-2 complex can interact with a cell membrane-anchored MT1-MMP. This proMMP-2 is then activated by an adjacent free MT1-MMP. To illustrate this process, it has been shown that proMMP-2 colocalizes with TIMP-2 and MT1-MMP inside caveolae on the surface of endothelial cells. Extracellular association of proMMP-2 and TIMP-2 depends on TIMP-2 phosphorylation by extracellular c-Src tyrosine kinase
-
tissue inhibitors of metalloproteinase 2
TIMP2
-
vitexin
interacts with enzyme residues Leu83, Ala84, His130, Pro140, Ala139, Met138, Ala, 136, Leu137, Thr143, Tyr142, Val117, His120, and Ile141, binding structure analysis, and modelling, overview
(2E)-3-(N-hydroxycarbamoyl)-2-(3-phenylpropylidene)propionyl-L-tryptophan-N-methylamide
-
-
(2E)-3-(N-hydroxycarbamoyl)-2-heptylidenepropionyl-L-tryptophan-N-methylamide
-
-
(2E)-3-(N-hydroxycarbamoyl)-2-isopropionyl-L-tryptophan-N-methylamide
-
-
(2E)-3-(N-hydroxycarbamoyl)-2-[(2E)-3-phenylprop-2-en-1-ylidene]propionyl-L-tryptophan-N-methylamide
-
-
(2E)-3-(N-hydroxycarbamoyl)-2-[(2E)-but-2-en-1-ylidene]propionyl-L-tryptophan-N-methylamide
-
-
(2R)-2-[(4-biphenylylcarbonyl)amino]-N-hydroxy-3-(1H-indol-3-yl)propionamide
-
-
(2R)-2-[(4-biphenylylsulfonyl)amino]-3-phenylpropionic acid
-
-
(2R)-2-[(4-biphenylylsulfonyl)amino]-3-phenylpropionic acid benzyl ester
-
-
(2R)-2-[[4-[benzenesulfonylhydrazonomethyl]benzenesulfonyl]-amino]-3-(1H-indol-3-yl)propionic acid methyl ester
-
-
(2R)-2-[[4-[benzenesulfonylhydrazonomethyl]benzenesulfonyl]-amino]-3-methylbutanoic acid tert-butyl ester
-
-
(2R)-2-[[5-(4-methoxyphenyl)thiophene-2-sulfonyl]-amino]-3-methylbutanoic acid
-
-
(2R)-2-[[5-(4-methoxyphenyl)thiophene-2-sulfonyl]-amino]-3-methylbutanoic acid methyl ester
-
-
(2R)-3-(1H-indol-3yl)-2-[[4-(phenylazo)benzenesulfonyl]amino]propionic acid
-
-
(2R)-3-(1H-indol-3yl)-2-[[4-[phenylaminocarbonyl]-benzenesulfonyl]amino]propionic acid benzyl ester
-
-
(2R)-3-methyl-2-[4-[phenoxybenzenesulfonyl]amino]butanoic acid
-
-
(2R)-3-methyl-2-[[4-[(4-nitrobenzoyl)-amino]benzenesulfonyl]amino]butanoic acid
-
-
(2R)-3-methyl-2-[[4-[(4-nitrobenzoyl)amino]benzenesulfonyl]amino]butanoic acid tert-butyl ester
-
-
(2R)-3-methyl-2-[[4-[2-[4-methylmercaptophenyl]-2H-tetrazol-5-yl]benzenesulfonyl]-amino]butanoic acid
-
-
(2R)-3-methyl-2-[[4-[2-[methylmercaptophenyl]-2H-tetrazol-5-yl]benzenesulfonyl]-amino]butanoic acid tert-butyl ester
-
-
(2R)-3-methyl-2-[[5-[(4-methylphenyl)ethynyl]thiophene-2-sulfonyl]-amino]butanoic acid methyl ester
-
-
(2R)-N-(benzyloxy)-2-[(4-biphenylsulfonyl)amino]-3-phenylpropionamide
-
-
(2R)-N-hydroxy-3-methyl-2-[(4-phenoxybenzenesulfonyl)amino]butanamide
-
-
(2R)-[(4-biphenylsulfonyl)amino]-N-hydroxy-3-phenylpropionamide
-
-
(4-phenoxyphenylsulfonyl)methylthiirane
-
selective inhibitor of MMP2
1,10-phenanthroline
1,4-dithiothreitol
-
-
2-(4-(4-[(2-thiiranylpropyl)sulfonyl]phenoxy)phenyl)acetic acid
-
selective inhibitor
2-([4-[3'-(2-aminoethoxy)-2-methylbiphenyl-4-yl]piperidin-1-yl]sulfonyl)-N-hydroxy-2-methylpropanamide
-
-
2-[(4-biphenyl-4-yl-3,6-dihydropyridin-1(2H)-yl)sulfonyl]-N-hydroxyacetamide
-
-
2-[(4-[3'-[2-(dimethylamino)ethoxy]-2-methylbiphenyl-4-yl]piperidin-1-yl)sulfonyl]-N-hydroxy-2-methylpropanamide
-
-
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
-
-
2-[[4-(2-chlorobiphenyl-4-yl)-3,6-dihydropyridin-1(2H)-yl]sulfonyl]-N-hydroxyacetamide
-
-
2-[[4-(2-ethylbiphenyl-4-yl)-3,6-dihydropyridin-1(2H)-yl]sulfonyl]-N-hydroxyacetamide
-
-
2-[[4-(2-fluorobiphenyl-4-yl)-3,6-dihydropyridin-1(2H)-yl]sulfonyl]-N-hydroxyacetamide
-
-
2-[[4-(3'-ethoxy-2-methylbiphenyl-4-yl)-3,6-dihydropyridin-1(2H)-yl]sulfonyl]-N-hydroxyacetamide
-
-
2-[[4-(3'-ethoxy-2-methylbiphenyl-4-yl)piperidin-1-yl]sulfonyl]-N-hydroxy-2-methylpropanamide
-
-
2-[[4-(3'-ethyl-2-methylbiphenyl-4-yl)-3,6-dihydropyridin-1(2H)-yl]sulfonyl]-N-hydroxyacetamide
-
-
4-(2-phenyl-2H-tetrazol-5-yl)benzenesulfonyl chloride
-
-
4-(3-phenylureido) benzenesulfonyl chloride
-
-
4-Aminobenzoyl-Gly-Pro-D-Leu-D-Ala-NHOH
-
-
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
-
-
D-tryptophan methyl ester tosylate
-
-
dibenzofuran-2-sulfonyl chloride
-
-
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
-
galardin
-
-
glycine
-
-
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
-
-
L-histidine
-
-
L-homocysteine
-
-
L-methionine
-
-
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
-
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
prostaglandin E2
PGE2, significantly increases MMP-2 activity as well as tube formation in endothelial cells. The PGE2-mediated elevation of MMP-2 activity is associated with the pro-angiogenic responses
tissue inhibitor of metalloproteinases-2
TIMP-2, a physiological inhibitor of MMPs. proMMP-2 can be secreted either in a free form or already complexed with TIMP-2 through its C-terminal domain. In the first case, a TIMP-2 that inhibits a cell membrane-anchored MT1-MMP by interaction between its N-terminal inhibitory domain and the catalytic domain of MT1-MMP, acts as a binding site for free proMMP-2 by interaction between the proMMP-2 Hpx-like domain and the TIMP-2 C-terminal domain. ProMMP-2 present in the resulting MT1-MMP-TIMP-2-proMMP-2 complex can then be activated by another adjacent TIMP-2-free MT1-MMP. In the second case, the N-terminal inhibitory domain of TIMP-2 in the proMMP-2-TIMP-2 complex can interact with a cell membrane-anchored MT1-MMP. This proMMP-2 is then activated by an adjacent free MT1-MMP. To illustrate this process, it has been shown that proMMP-2 colocalizes with TIMP-2 and MT1-MMP inside caveolae on the surface of endothelial cells. Extracellular association of proMMP-2 and TIMP-2 depends on TIMP-2 phosphorylation by extracellular c-Src tyrosine kinase
-
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
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.3 - 2.5
peptide A13
-
0.1 - 0.4
peptide A13R
-
1.2 - 3.6
peptide A3
-
2.2 - 4.3
peptide A34
-
0.2 - 2.2
peptide B74
-
0.9 - 4.4
peptide C9
-
0.136 - 0.172
Ac-Pro-Leu-Gly-[2-mercapto-4-methylpentanoyl]-Leu-Gly-OEt
0.134
Acetyl-Pro-Leu-Gly-thioester-Leu-Leu-Gly ethyl ester
-
gelatinase A synthetic 19000 MW catalytic domain
0.0044
alpha1(V)436-447 fTHP
-
pH 7.5, 30°C
-
0.059 - 0.118
Dnp-Pro-beta-cyclohexyl-Ala-Gly-Cys(Me)-His-Ala-Lys(N-Me-Abz)-NH2
0.159
fibrinogen
-
cleavage of the alpha-chain of the native substrate, full-length MMP-2, pH 7.1, 37°C
-
0.0172
fTHP-3
-
pH 7.5, 30°C
-
15
Gly-Pro-Gln-Gly-Ile-Ala-Gly-Gln
-
-
3.4
Gly-Pro-Gln-Gly-Ile-Ala-Ser-Gln
-
-
4.8
Gly-Pro-Gln-Gly-Ile-Phe-Gly-Gln
-
-
1.1
Gly-Pro-Gln-Gly-Ile-Trp-Gly-Gln
-
-
0.0057 - 0.0099
Mca-Pro-Leu-Gly-Leu-Dap-Ala-Arg-NH2
0.00152 - 0.00306
MOAcPLGLA2pr(Dnp)-AR-NH2
1.3
peptide A13
-
pH 7.5, 37°C
-
0.4
peptide A13P, peptide A13R
-
pH 7.5, 37°C
-
7.7
peptide A21
-
pH 7.5, 37°C
-
3.2
peptide A21A
-
pH 7.5, 37°C
-
3.6
peptide A3
-
pH 7.5, 37°C
-
2.2
peptide A34
-
pH 7.5, 37°C
-
2.4
peptide B37
-
pH 7.5, 37°C
-
4.5
peptide B49
-
pH 7.5, 37°C
-
2.2
peptide B74
-
pH 7.5, 37°C
-
0.6
peptide B74P
-
pH 7.5, 37°C
-
0.8
peptide B74R
-
pH 7.5, 37°C
-
4.4
peptide C9
-
pH 7.5, 37°C
-
6.4
peptide C9R
-
pH 7.5, 37°C
-
0.0085
type I collagen
-
pH 7.5, 25°C
-
0.0012
vitronectin of MW 65000
-
-
-
0.001
vitronectin of MW 75000
-
-
-
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
31 - 105
peptide A13
-
2 - 18
peptide A13R
-
73 - 400
peptide A3
-
60 - 202
peptide A34
-
17 - 622
peptide B74
-
26 - 740
peptide C9
-
16.7 - 19.5
Ac-Pro-Leu-Gly-[2-mercapto-4-methylpentanoyl]-Leu-Gly-OEt
1.6
Acetyl-Pro-Leu-Gly-thioester-Leu-Leu-Gly ethyl ester
-
-
0.0616
alpha1(V)436-447 fTHP
-
pH 7.5, 30°C
-
4.7 - 5.4
Dnp-Pro-beta-cyclohexyl-Ala-Gly-Cys(Me)-His-Ala-Lys(N-Me-Abz)-NH2
36.4
fibrinogen
-
cleavage of the alpha-chain of the native substrate, full-length MMP-2, pH 7.1, 37°C
-
0.017
fTHP-3
-
30°C
-
2.69
Gly-Pro-Gln-Gly-Ile-Ala-Gly-Gln
-
-
2
Gly-Pro-Gln-Gly-Ile-Ala-Ser-Gln
-
-
3.33
Gly-Pro-Gln-Gly-Ile-Phe-Gly-Gln
-
-
0.612
Gly-Pro-Gln-Gly-Ile-Trp-Gly-Gln
-
-
0.6 - 1.7
Mca-Pro-Leu-Gly-Leu-Dap-Ala-Arg-NH2
1.3 - 6
MOAcPLGLA2pr(Dnp)-AR-NH2
105
peptide A13
-
pH7.5, 37°C
-
204
peptide A13P
-
pH7.5, 37°C
-
2 - 8
peptide A13R
-
pH7.5, 37°C
-
124
peptide A21
-
pH7.5, 37°C
-
601
peptide A21A
-
pH7.5, 37°C
-
400
peptide A3
-
pH7.5, 37°C
-
202
peptide A34
-
pH7.5, 37°C
-
353
peptide B37
-
pH7.5, 37°C
-
510
peptide B49
-
pH7.5, 37°C
-
622
peptide B74
-
pH7.5, 37°C
-
264
peptide B74P
-
pH7.5, 37°C
-
61
peptide B74R
-
pH7.5, 37°C
-
740
peptide C9
-
pH7.5, 37°C
-
0.0045
type I collagen
-
pH 7.5, 25°C
-
0.0022
type V collagen
-
pH 7.5, 32°C
-
0.00167
vitronectin of MW 65000 and 75000
-
-
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
30000
LS276-THP
-
pH 7.4, 37°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00000000068
APP-IP-TIMP-2
pH 7.5, 37°C
-
0.00046
2-(4-(4-[(2-thiiranylpropyl)sulfonyl]phenoxy)phenyl)acetic acid
-
-
0.00005
methyl 2-(4-(4-[(2-thiiranylpropyl)-sulfonyl]phenoxy)phenyl)acetate
-
-
0.0000097
TIMP-1
-
pH 8.0, 25°C, 62 kDa form
-
0.0000072 - 0.0011
TIMP-2
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00028
(2E)-3-(N-hydroxycarbamoyl)-2-(3-phenylpropylidene)propionyl-L-tryptophan-N-methylamide
Homo sapiens
-
-
0.000123
(2E)-3-(N-hydroxycarbamoyl)-2-heptylidenepropionyl-L-tryptophan-N-methylamide
Homo sapiens
-
-
0.0000092
(2E)-3-(N-hydroxycarbamoyl)-2-isopropionyl-L-tryptophan-N-methylamide
Homo sapiens
-
-
0.00012
(2E)-3-(N-hydroxycarbamoyl)-2-[(2E)-3-phenylprop-2-en-1-ylidene]propionyl-L-tryptophan-N-methylamide
Homo sapiens
-
-
0.0785
(2E)-3-(N-hydroxycarbamoyl)-2-[(2E)-but-2-en-1-ylidene]propionyl-L-tryptophan-N-methylamide
Homo sapiens
-
-
0.000188
2-([4-[3'-(2-aminoethoxy)-2-methylbiphenyl-4-yl]piperidin-1-yl]sulfonyl)-N-hydroxy-2-methylpropanamide
Homo sapiens
-
-
0.000009
2-[(4-biphenyl-4-yl-3,6-dihydropyridin-1(2H)-yl)sulfonyl]-N-hydroxyacetamide
Homo sapiens
-
-
0.000534
2-[(4-[3'-[2-(dimethylamino)ethoxy]-2-methylbiphenyl-4-yl]piperidin-1-yl)sulfonyl]-N-hydroxy-2-methylpropanamide
Homo sapiens
-
-
0.000776
2-[[4-(2,3'-dimethylbiphenyl-4-yl)-3,6-dihydropyridin-1(2H)-yl]sulfonyl]-N-hydroxyacetamide
Homo sapiens
-
-
0.00062
2-[[4-(2-chlorobiphenyl-4-yl)-3,6-dihydropyridin-1(2H)-yl]sulfonyl]-N-hydroxyacetamide
Homo sapiens
-
-
0.00438
2-[[4-(2-ethylbiphenyl-4-yl)-3,6-dihydropyridin-1(2H)-yl]sulfonyl]-N-hydroxyacetamide
Homo sapiens
-
-
0.000017
2-[[4-(2-fluorobiphenyl-4-yl)-3,6-dihydropyridin-1(2H)-yl]sulfonyl]-N-hydroxyacetamide
Homo sapiens
-
-
0.000998
2-[[4-(3'-ethoxy-2-methylbiphenyl-4-yl)-3,6-dihydropyridin-1(2H)-yl]sulfonyl]-N-hydroxyacetamide
Homo sapiens
-
-
0.000457
2-[[4-(3'-ethoxy-2-methylbiphenyl-4-yl)piperidin-1-yl]sulfonyl]-N-hydroxy-2-methylpropanamide
Homo sapiens
-
-
0.001208
2-[[4-(3'-ethyl-2-methylbiphenyl-4-yl)-3,6-dihydropyridin-1(2H)-yl]sulfonyl]-N-hydroxyacetamide
Homo sapiens
-
-
0.141
ascorbic acid
Homo sapiens
-
recombinant enzyme
0.195
GSH
Homo sapiens
-
recombinant enzyme
0.547
GSSG
Homo sapiens
-
recombinant enzyme
0.0000005 - 0.0000011
ilomastat
0.0073 - 0.015
ISYGNDALMP
Homo sapiens
-
pH 7.5, 37°C, recombinant fragments of MMP-2
0.061
L-cysteine
Homo sapiens
-
recombinant enzyme
0.118
L-histidine
Homo sapiens
-
recombinant enzyme
0.727
L-homocysteine
Homo sapiens
-
recombinant enzyme
8.68
L-methionine
Homo sapiens
-
recombinant enzyme
1
N-acetylcysteine
Homo sapiens
-
recombinant enzyme
0.00308
N-hydroxy-2-([4-[2-(trifluoromethyl)biphenyl-4-yl]-3,6-dihydropyridin-1(2H)-yl]sulfonyl)acetamide
Homo sapiens
-
-
0.000173
N-hydroxy-2-([4-[2-methyl-3'-(trifluoromethoxy)biphenyl-4-yl]-3,6-dihydropyridin-1(2H)-yl]sulfonyl)acetamide
Homo sapiens
-
-
0.000262
N-hydroxy-2-([4-[3'-(2-hydroxyethoxy)-2-methylbiphenyl-4-yl]piperidin-1-yl]sulfonyl)-2-methylpropanamide
Homo sapiens
-
-
0.000853
N-hydroxy-2-([4-[3'-(2-methoxyethoxy)-2-methylbiphenyl-4-yl]piperidin-1-yl]sulfonyl)-2-methylpropanamide
Homo sapiens
-
-
0.000196
N-hydroxy-2-([4-[3'-(methoxymethyl)-2-methylbiphenyl-4-yl]-3,6-dihydropyridin-1(2H)-yl]sulfonyl)acetamide
Homo sapiens
-
-
0.000196
N-hydroxy-2-methyl-2-[(4-[2-methyl-3'-[2-(methylamino)ethoxy]biphenyl-4-yl]piperidin-1-yl)sulfonyl]propanamide
Homo sapiens
-
-
0.000529
N-hydroxy-2-[(4-[4-[6-(2-hydroxyethoxy)pyridin-2-yl]-3-methylphenyl]piperidin-1-yl)sulfonyl]-2-methylpropanamide
Homo sapiens
-
-
0.00032
N-hydroxy-2-[[4-(2-methylbiphenyl-4-yl)-3,6-dihydropyridin-1(2H)-yl]sulfonyl]acetamide
Homo sapiens
-
-
0.000222
N-hydroxy-2-[[4-(3'-methoxy-2-methylbiphenyl-4-yl)-3,6-dihydropyridin-1(2H)-yl]sulfonyl]acetamide
Homo sapiens
-
-
0.01
peptide P713
Homo sapiens
-
pH 7.0, 22°C
-
0.0342
UK-370106
Homo sapiens
-
-
additional information
additional information
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.368
-
GaCDfn, with fibronectin-like insert
11.8
-
GaCD, without fibronectin-like insert
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5 - 7.6
assay at
7.4
-
assay at
8.5
-
azocoll
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 10
-
-
5.5 - 9
-
gelatinase A synthetic 19000 MW catalytic domain
6 - 9
-
pH 6.0: about 40% of activity maximum, pH 9.0: about 85% of activity maximum, azocoll
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
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 22
assay at
22
-
assay at
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.64
2D electrophoresis
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
the enzyme is overexpressed in tumors, it is expressed in all tumors tested
Manually annotated by BRENDA team
higher intensity of staining of MMP-2 is observed in regions of invasion of the muscularis mucosa compared with superficial portions of the tumor in colorectal cancer
Manually annotated by BRENDA team
oxytalan fibers
Manually annotated by BRENDA team
from periodontal ligaments
Manually annotated by BRENDA team
distribution and activation of matrix metalloproteinase-2 in skeletal muscle fibers, quantification of MMP2 in muscle, overview
Manually annotated by BRENDA team
Mycobacterium tuberculosis stimulates matrix metalloproteinases secretion in the host. Analysis of the patterns of matrix metalloproteinase 9 (MMP-9) and 2 (MMP-2) isoforms in sputum samples, overview
Manually annotated by BRENDA team
-
demineralized dentin matrix, extraction is best at acidic conditions of pH 2-3 compared to pH 7.4-EDTA-containing extracts
Manually annotated by BRENDA team
-
nucleus pulposus of intervertebral disc
Manually annotated by BRENDA team
-
tumor periphery
Manually annotated by BRENDA team
-
HSC-180 cell
Manually annotated by BRENDA team
-
leukemia cell line, secretion of MMP-2
Manually annotated by BRENDA team
-
derived from premenopausal women aged 45-55 years who underwent total abdominal hysterectomy
Manually annotated by BRENDA team
-
stimulated, release of MMP-2 in vitro
Manually annotated by BRENDA team
-
plasma prepared from blood emerging from a skin wound inflicted for the measurement of the bleeding time, shed blood, and simultaneously from venous blood in 27 healthy human volunteers, with and without treatment of the individuals with acetylsalicylic acid before. MMP-2 activity is higher in shed blood. Acetylsalicylic acid has no effect on MMP-2 secretion, overview
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
tissue samples of oral squamous cell carcinomas
Manually annotated by BRENDA team
-
fibroids of different size show equal MMP-2 activity
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
besides MT-MMPs, which efficiently bind proMMP-2 to induce its activation, a limited number of cell-surface molecules have been shown to contribute to enhance proteolytic activity at the migrating front of invasive cells by clustering active MMP-2 at the cell membrane. Among them the heat shock protein HSP90a expressed at the surface of tumor cells promotes MMP-2 activity and tumor invasion by binding to the Hpx-like domain of MMP-2. The alphanybeta3 integrin is first identified as a binding site for the C-terminal Hpx-like domain of MMP-2 in studies investigating in vivo and in vitro interactions between angiogenic blood vessels and melanoma cells
Manually annotated by BRENDA team
-
main localization in invertebral disc, immunohistochemic analysis, overview
Manually annotated by BRENDA team
additional information
the enzyme sequence contains a 29-residues-signal peptide responsible for translocation to the endoplasmic reticulum. Secreted enzyme MMP-2 can be endocytosed through direct or indirect binding to several membrane proteins, translocation across the endosome membrane towards the cytosol. Besides its transient journey in the secretory pathway (endoplasmic reticulum, Golgi apparatus and related vesicles), intracellular MMP-2 is not restricted to the cytosol but is also found in organelles including nucleus and mitochondria. proMMP-2 can be secreted either in a free form or already complexed with TIMP-2 through its C-terminal domain. LRP-2 is able to bind and endocytose proMMP-2 complexed to TIMP-2
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
MMP-2 is a member of the matrix metalloproteinase family
malfunction
physiological function
malfunction
-
the inactivation of the MMP-2 gene prevents thrombosis induced by weak, but not strong, stimuli but produces only a moderate prolongation of the bleeding time. MMP-2 deficient mice have hyporeactive platelets, a defective thrombotic response and mildly impaired hemostasis
physiological function
-
platelet-derived MMP-2 facilitates thrombus formation
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
MMP2_HUMAN
660
0
73882
Swiss-Prot
Secretory Pathway (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
64000
x * 72000, native proMMP-2, x * 64000, recombinant MMP-2
72000
20000
-
GaCD, without fibronectin-like insert, SDS-PAGE
25920
-
recombinant C domain, elektrospray mass spectrometry
26500
-
recombinant C domain, SDS-PAGE
38000
-
GaCDfn, with fibronectin-like insert, SDS-PAGE
45000
-
active form lacking the C-terminal domain, SDS-PAGE
47052
-
x * 66000, SDS-PAGE, x * 66518, calculated, enzyme mutant E404A, x * 59000, SDS-PAGE, x * 47052, calculated, enzyme mutant lacking collagen-binding domain
57000
-
x * 57000, human, active form, SDS-PAGE
59000
-
x * 66000, SDS-PAGE, x * 66518, calculated, enzyme mutant E404A, x * 59000, SDS-PAGE, x * 47052, calculated, enzyme mutant lacking collagen-binding domain
62000
66000
66518
-
x * 66000, SDS-PAGE, x * 66518, calculated, enzyme mutant E404A, x * 59000, SDS-PAGE, x * 47052, calculated, enzyme mutant lacking collagen-binding domain
67000
-
x * 67000, human, active form, SDS-PAGE under reducing condition
68000
72000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
homodimerization of enzyme MMP-2, through an intermolecular disulfide bond between Cys102 and the neighboring Cys102, requires Ca2+ but is not associated with protein kinase C-mediated phosphorylation. The cleavage is followed by intermolecular autoproteolytic cleavage at the Asn109-Tyr peptide bond, resulting in full enzymatic activation. Homodimerization of the enzyme enhances thrombin-mediated activation of pro-MMP-2
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
proMMP-2 contains 29 potential phosphorylation sites, that at least five of these sites are phosphorylated, purified MMP-2 is phosphorylated by protein kinase C in vitro, peptide mass fingerprint for phosphorylation site determination, overview
proteolytic modification
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C102S
site-directed mutagenesis
C233S
site-directed mutagenesis
C247S
site-directed mutagenesis
C259S
site-directed mutagenesis
C274S
site-directed mutagenesis
C291S
site-directed mutagenesis
C305S
site-directed mutagenesis
C317S
site-directed mutagenesis
C332S
site-directed mutagenesis
C349S
site-directed mutagenesis
C363S
site-directed mutagenesis
C375S
site-directed mutagenesis
C395S
site-directed mutagenesis
C60S
site-directed mutagenesis
C65S
site-directed mutagenesis
E404A
proteolytically inactive pro-MMP-2 mutant
E412D
site-directed mutagenesis
S160A
site-directed mutagenesis
S365A
site-directed mutagenesis
S575A
site-directed mutagenesis
S644A
site-directed mutagenesis
S647A
site-directed mutagenesis
T250A
site-directed mutagenesis
T354A
site-directed mutagenesis
T377A/T378A
site-directed mutagenesis
T455A
site-directed mutagenesis
T73A
site-directed mutagenesis
T96A
site-directed mutagenesis
A404E
-
inactive
D49A
-
site-directed mutagenesis
E404A
-
no enzymic activity, competition with isolated collagen-binding domain and with matrix metalloproteinase MMP-9 binding to native and denatured type I collagen
K50G
-
site-directed mutagenesis
K50R
-
site-directed mutagenesis
R19L
-
site-directed mutagenesis
R19L/R38L
-
site-directed mutagenesis
R38L
-
site-directed mutagenesis
Y25A
-
site-directed mutagenesis
Y37A
-
site-directed mutagenesis
Y46A
-
site-directed mutagenesis
Y52A
-
site-directed mutagenesis
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60.8
-
Tm
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
the plasmatic half-life of human recombinant pro-MMP-2, assessed after the intravenous injection of 500 ng of the proenzyme in MMP-2-deficient mice is 19 min
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
catalytic domain of mutated enzyme
native, extracellular, inhibitor-free enzyme from glioblastoma cell line T98G cell culture medium
recombinant enzyme
recombinant enzyme from HeLa S3 cells, native enzyme purified from HT-1080 cells
recombinant soluble enzyme from Escherichia coli cell-free extract by gelatin affinity chromatography
as an inactive zymogen, rapid activation by 4-aminophenylmercuric acetate
-
catalytic domain
-
col-1 module
-
native MMP-2 from dentin inculding serial dilutions, method development
-
purification procedure
-
recombinant C domain
-
recombinant CBD1, CBD2 and CBD3 polypeptides and fibronectin type-II-like modelues of MMP-2 from Escherichia coli, by gelatin affinity chromatography
-
recombinant enzyme
-
recombinant His-tagged enzyme without pro-domain and isolated MMP-2 CBD domain from Escherichia coli inclusion bodies, after solubilization and refolding, by nickel affinity chromatography
-
recombinant pro-gelatinase A
-
recombinant proMMP-2 expressed in Sf9 cells
-
second fibronectin type II module, residues 278-336, produced in Escherichia coli
-
solubilized, refolded recombinant GST-tagged MMP-2 by glutathione affinity chromatography, removal of the tag
-
truncated MMP-2 catalytic domain MMP-2C
-
with or without fibronectin-like insert
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cDNA of the mutated enzyme used to transfect HEK 293 cells
gene MMP-2, quantitative real time PCR expression analysis in glioblastoma
gene MMP2, genotyping in Tunesian population. The levels of MMP-2 mRNA expression in patients containing the CC genotype are much higher compared with cells with the CT genotype. The frequency of the MMP-2 CC genotype is significantly higher in colorectal cancer patients when compared with controls
gene MMP2, sequence comparisons, enzyme expression analysis
gene MMP2, the gene is located on the long arm of chromosome 16 at position q12.2, the cDNA for MMP-2 codes for a 660 residues preproenzyme containing a 29 residues signal peptide responsible for translocation to the endoplasmic reticulum and followed by the 72-kDa-proenzyme. The human MMP2 gene lacks a conventional TATA-box or classical transcription response elements found in other MMP genes, the constitutive expression depends on p53-, Sp1-, Sp3-and AP-2-binding sites but the promoter contains other cis-regulatory elements including C/EBP, ATF2, PEA3/Ets, c-myc and AP-1 binding sites. Transcriptionally active MMP-2 in invasive cancer cells is characterized by hypomethylation of CpG regions in the MMP2 promoter and low levels of histone H3 lysine-27 trimethylation
pro-MMP-2 expressed in a recombinant vaccinia virus mammalian cell expression system
recombinant enzyme from HeLa S3 cells infected with vaccinia virus encoding the full-length cDNA of pro-MMP-2
recombinant expression of soluble and functional full-length enzyme from plasmid pET5a-MMP-2 in the cytoplasm of Escherichia coli strain BL21(DE3)/pLysS, subcloning in Escherichia coli strain DH5alpha, method development and evaluation, overview
recombinant expression of wild-type and mutant full-length MMP-2 or MMP-2 with C-terminal Myc and His tags in COS-1 cells, secretion of the enzyme to the cell culture medium
cDNA cloned and expressed in Escherichia coli JM-109
-
cDNA, recombinant C domain expressed in Escherichia coli
-
cloned and expressed in Escherichia coli
-
cloned and overexpressed in a bacterial system, Escherichia coli BL21(DE3)pLysS
-
expression of GST-tagged MMP-2 in Escherichia coli strain DH5alpha in inclusion bodies
-
expression of His- and myc-tagged pro-MMP-2
-
expression of the first, second, and third module, i.e. CBD1, CBD2 and CBD3 polypeptides, and of the fibronectin type-II-like modelues of MMP-2 in Escherichia coli
-
expression of the His-tagged enzyme without pro-domain and of the isolated MMP-2 CBD domain in Escherichia coli in inclusion bodies
-
full-length progelatinase A
-
MMP-2 expression analysis in SK-Hep1 hepatoma cells, overview
-
pro-gelatinase A in transfected mammalian cell lines
-
recombinant proMMP-2 expressed in Sf9 cells
-
second fibronectin type II module, residues 278-336, produced in Escherichia coli
-
truncated MMP-2 catalytic domain MMP-2C
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
Mycobacterium tuberculosis stimulates matrix metalloproteinases secretion in the host
significant progressive increase in total MMP-2 plasma levels with progression from adenomatous polyps through advancing Dukes stages
expression and activity of MMP-2 is 6fold induced by osteopontin through binding to integrin avb3 and CD44v6 in hepatocellular carcinoma cells SMMC7721 and HepG2
-
inhibition of the SDF-1a/CXCR4 axis downregulates the rhOPN-induced MMP-2 expression and activity
-
matrix metalloproteinase 2 activity decreases in human periodontal ligament fibroblast cultures submitted to simulated orthodontic force by centrifugation (141xg) for 30, 60, 90, and 120 min at 24 h regardless of the duration of centrifugation and at 48 h in cells centrifuged for 30 min only
-
profibrogenic gene expression of MMP-2 is down-regulated (75% decrement) in response to adenoviral delivery of dominant-negative transforming growth factor beta type II receptor in hepatic stellate cells
-
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
recombinant GST-tagged enzyme from Escherichia coli inclusion bodies by solubilization of the inclusion bodies with guanidine-HCl followed by refolding by rapid dilution method
-
solubilization of recombinant His-tagged enzyme without pro-domain and isolated MMP-2 CBD domain from Escherichia coli inclusion bodies with 8 M urea, 0.1 M NaH2PO4 and 0.01 M Tris-HCl, pH 8.0, followed by refolding
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
diagnostics
-
assessment of enzyme for monitoring and screening patients with prostate cancer. Significant correlation of densitometric analysis of enzyme activity and indirect hemagglutination titer, and prostate-specific antigen parameters
medicine
additional information
-
in patients with degenerative disc disease, proenzyme levels in nucleus pulposus of intervertebral disc are higher at early stages of the disease. Proenzyme and tissue inhibitor of metalloproteinase-2 levels negatively correlate in herniated disc samples, and proenzyme levels negatively correlate with the collagen content
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Netzel-Arnett, S.; Sang, Q.X.; Moore, W.G.I.; Navre, M.; Birkedal-Hansen, H.; van Wart, H.E.
Comparative sequence specificities of human 72- and 92-kDa gelatinases (type IV collagenases) and PUMP (matrilysin)
Biochemistry
32
6427-6432
1993
Homo sapiens
Manually annotated by BRENDA team
Okada, Y.; Morodomi, T.; Enghild, J.J.; Suzuki, K.; Yasui, A.; Nakanishi, I.; Salvesen, G.; Nagase, H.
Matrix metalloproteinase 2 from human rheumatoid synovial fibroblasts. Purification and activation of the precursor and enzymic properties
Eur. J. Biochem.
194
721-730
1990
Homo sapiens
Manually annotated by BRENDA team
Collier, I.E.; Wilhelm, S.M.; Eisen, A.Z.; Marmer, B.L.; Grant, G.A.; Seltzer, J.L.; Kronberger, A.; He, C.; Bauer, E.A.; Goldberg, G.I.
H-ras oncogene-transformed human bronchial epithelial cells (TBE-1) secrete a single metalloprotease capable of degrading basement membrane collagen
J. Biol. Chem.
263
6579-6587
1988
Homo sapiens
Manually annotated by BRENDA team
Nguyen, Q.; Murphy, G.; Hughes, C.E.; Mort, J.S.; Roughley, P.J.
Matrix metalloproteinases cleave at two distinct sites on human cartilage link protein
Biochem. J.
295
595-598
1993
Homo sapiens
Manually annotated by BRENDA team
Ochieng, J.; Fridman, R.; Nangia-Makker, P.; Kleiner, D.E.; Liotta, L.A.; Stetler-Stevenson, W.G.; Raz, A.
Galectin-3 is a novel substrate for human matrix metalloproteinases-2 and -9
Biochemistry
33
14109-14114
1994
Homo sapiens
Manually annotated by BRENDA team
Allan, J.A.; Docherty, A.J.P.; Barker, P.J.; Huskisson, N.S.; Reynolds, J.J.; Murphy, G.
Binding of gelatinases A and B to type-I collagen and other matrix components
Biochem. J.
309
299-306
1995
Homo sapiens
Manually annotated by BRENDA team
Imai, K.; Shikata, H.; Okada, Y.
Degradation of vitronectin by matrix metalloproteinases-1, -2, -3, -7 and -9
FEBS Lett.
369
249-251
1995
Homo sapiens
Manually annotated by BRENDA team
Fridman, R.; Bird, R.E.; Hoyhta, M.; Oelkuct, M.; Komarek, D.; Liang, C.M.; Berman, M.L.; Liotta, L.A.; Stetler-Stevenson, W.G.; Fuerst, T.R.
Expression of human recombinant 72 kDa gelatinase and tissue inhibitor of metalloproteinase-2 (TIMP-2): characterization of complex and free enzyme
Biochem. J.
289
411-416
1993
Homo sapiens
Manually annotated by BRENDA team
Willenbrock, F.; Crabbe, T.; Slocombe, P.M.; Sutton, C.W.; Docherty, A.J.P.; Cockett, M.I.; O'Shea, M.; Brocklehurst, K.; Phillips, I.R.; Murphy, G.
The activity of the tissue inhibitors of metalloproteinases is regulated by C-terminal domain interactions: a kinetic analysis of the inhibition of gelatinase A
Biochemistry
32
4330-4337
1993
Homo sapiens
Manually annotated by BRENDA team
Miyazaki, K.; Funahashi, K.; Numata, Y.; Koshikawa, N.; Akaogi, K.; Kikkawa, Y.; Yasumitsu, H.; Umeda, M.
Purification and characterization of a two-chain form of tissue inhibitor of metalloproteinases (TIMP) type 2 and a low molecular weight TIMP-like protein
J. Biol. Chem.
268
14387-14393
1993
Homo sapiens
Manually annotated by BRENDA team
Banyai, L.; Tordai, H.; Patthy, L.
The gelatin-binding site of human 72 kDa type IV collagenase (gelatinase A)
Biochem. J.
298
403-407
1994
Homo sapiens
Manually annotated by BRENDA team
Ye, Q.Z.; Johnson, L.L.; Yu, A.E.; Hupe, D.
Reconstructed 19 kDa catalytic domain of gelatinase A is an active proteinase
Biochemistry
34
4702-4708
1995
Homo sapiens
Manually annotated by BRENDA team
LePage, R.N.; Fosang, A.J.; Fuller, S.J.; Murphy, G.; Evin, G.; Beyreuther, K.; Masters, C.L.; Small, D.H.
Gelatinase A possesses a beta-secretase-like activity in cleaving the amyloid protein precursor of Alzheimers disease
FEBS Lett.
377
267-270
1995
Homo sapiens
Manually annotated by BRENDA team
Gohlke, U.; Gomis-Ruth, F.X.; Crabbe, T.; Murphy, G.; Docherty, A.J.P.; Bode, W.
The C-terminal (haemopexin-like) domain structure of human gelatinase A (MMP2): structural implications for its function
FEBS Lett.
378
126-130
1996
Homo sapiens
Manually annotated by BRENDA team
Libson, A.M.; Gittis, A.G.; Collier, I.E.; Marmer, B.L.; Goldberg, G.I.; Lattman, E.E.
Crystal structure of the haemopexin-like C-terminal domain of gelatinase A [letter]
Nat. Struct. Biol.
2
938-942
1995
Homo sapiens
Manually annotated by BRENDA team
Murphy, G.; Crabbe, T.
Gelatinases A and B
Methods Enzymol.
248
470-484
1995
Homo sapiens
Manually annotated by BRENDA team
Fridman, R.; Toth, M.; Pena, D.; Mobashery, S.
Activation of progelatinase B (MMP-9) by gelatinase A (MMP-2)
Cancer Res.
55
2548-2555
1995
Homo sapiens
Manually annotated by BRENDA team
Lee, H.J.; Chung, M.C.; Lee, C.H.; Chun, H.K.; Kho, Y.H.
Purification of progelatinase A (matrix metalloproteinase 2) and a tissue inhibitor of metalloproteinase-2 (TIMP-2) from T98G human glioblastoma cells
J. Biochem. Mol. Biol.
28
33-39
1995
Homo sapiens
-
Manually annotated by BRENDA team
Ochieng, J.; Warfield, P.; Green, B.
Interactions of gelatinases with soluble and immobilized fetuin and asialofetuin
Arch. Biochem. Biophys.
322
250-255
1995
Homo sapiens
Manually annotated by BRENDA team
Hutton, M.; Willenbrock, F.; Brocklehurst, K.; Murphy, G.
Kinetic analysis of the mechanism of interaction of full-length TIMP-2 and gelatinase A: evidence for the existence of a low-affinity intermediate
Biochemistry
37
10094-10098
1998
Homo sapiens
Manually annotated by BRENDA team
Feng, Y.; Likos, J.J.; Zhu, L.; Woodward, H.; Munie, G.; McDonald, J.J.; Stevens, A.M.; Howard, C.P.; De Crescenzo, G.A.; Welsch, D.; Shieh, H.S.; Stallings, W.C.
Solution structure and backbone dynamics of the catalytic domain of matrix metalloproteinase-2 complexed with a hydroxamic acid inhibitor
Biochim. Biophys. Acta
1598
10-23
2002
Homo sapiens
Manually annotated by BRENDA team
Gehrmann, M.; Briknarova, K.; Banyai, L.; Patthy, L.; Llinas, M.
The col-1 module of human matrix metalloproteinase-2 (MMP-2): structural/functional relatedness between gelatin-binding fibronectin type II modules and lysine-binding kringle domains
Biol. Chem.
383
137-148
2002
Homo sapiens
Manually annotated by BRENDA team
Collier, I.E.; Saffarian, S.; Marmer, B.L.; Elson, E.L.; Goldberg, G.
Substrate recognition by gelatinase A: the C-terminal domain facilitates surface diffusion
Biophys. J.
81
2370-2377
2001
Homo sapiens
Manually annotated by BRENDA team
Tordai, H.; Patthy, L.
The gelatin-binding site of the second type-II domain of gelatinase A/MMP-2
Eur. J. Biochem.
259
513-518
1999
Homo sapiens
Manually annotated by BRENDA team
Lee, S.J.; Jang, J.W.; Kim, Y.M.; Lee, H.I.; Jeon, J.Y.; Kwon, Y.G.; Lee, S.T.
Endostatin binds to the catalytic domain of matrix metalloproteinase-2
FEBS Lett.
519
147-152
2002
Homo sapiens
Manually annotated by BRENDA team
Bigg, H.F.; Shi, Y.E.; Liu, Y.E.; Steffensen, B.; Overall, C.M.
Specific, high affinity binding of tissue inhibitor of metalloproteinases-4 (TIMP-4) to the COOH-terminal hemopexin-like domain of human gelatinase A. TIMP-4 binds progelatinase A and the COOH-terminal domain in a similar manner to TIMP-2
J. Biol. Chem.
272
15496-15500
1997
Homo sapiens
Manually annotated by BRENDA team
Olson, M.W.; Gervasi, D.C.; Mobashery, S.; Fridman, R.
Kinetic analysis of the binding of human matrix metalloproteinase-2 and -9 to tissue inhibitor of metalloproteinase (TIMP)-1 and TIMP-2
J. Biol. Chem.
272
29975-29983
1997
Homo sapiens
Manually annotated by BRENDA team
Wallon, U.M.; Overall, C.M.
The hemopexin-like domain (C domain) of human gelatinase A (matrix metalloproteinase-2) requires Ca2+ for fibronectin and heparin binding. Binding properties of recombinant gelatinase A C domain to extracellular matrix and basement membrane components
J. Biol. Chem.
272
7473-7481
1997
Homo sapiens
Manually annotated by BRENDA team
Kleifeld, O.; Kotra, L.P.; Gervasi, D.C.; Brown, S.; Bernardo, M.M.; Fridman, R.; Mobashery, S.; Sagi, I.
X-ray absorption studies of human matrix metalloproteinase-2 (MMP-2) bound to a highly selective mechanism-based inhibitor. comparison with the latent and active forms of the enzyme
J. Biol. Chem.
276
17125-17131
2001
Homo sapiens (P08253), Homo sapiens
Manually annotated by BRENDA team
Chen, E.I.; Kridel, S.J.; Howard, E.W.; Li, W.; Godzik, A.; Smith, J.W.
A unique substrate recognition profile for matrix metalloproteinase-2
J. Biol. Chem.
277
4485-4491
2002
Homo sapiens
Manually annotated by BRENDA team
Higashi, S.; Miyazaki, K.
Identification of a region of beta-amyloid precursor protein essential for its gelatinase A inhibitory activity
J. Biol. Chem.
278
14020-14028
2003
Homo sapiens
Manually annotated by BRENDA team
Chen, E.I.; Li, W.; Godzik, A.; Howard, E.W.; Smith, J.W.
A residue in the S2 subsite controls substrate selectivity of matrix metalloproteinase-2 and matrix metalloproteinase-9
J. Biol. Chem.
278
17158-17163
2003
Homo sapiens (P08253)
Manually annotated by BRENDA team
Lauer-Fields, J.L.; Sritharan, T.; Stack, M.S.; Nagase, H.; Fields, G.B.
Selective hydrolysis of triple-helical substrates by matrix metalloproteinase-2 and -9
J. Biol. Chem.
278
18140-18145
2003
Homo sapiens
Manually annotated by BRENDA team
Rosenblum, G.; Meroueh, S.O.; Kleifeld, O.; Brown, S.; Singson, S.P.; Fridman, R.; Mobashery, S.; Sagi, I.
Structural basis for potent slow binding inhibition of human matrix metalloproteinase-2 (MMP-2)
J. Biol. Chem.
278
27009-27015
2003
Homo sapiens (P08253), Homo sapiens
Manually annotated by BRENDA team
Tamura, Y.; Watanabe, F.; Nakatani, T.; Yasui, K.; Fuji, M.; Komurasaki, T.; Tsuzuki, H.; Maekawa, R.; Yoshioka, T.; Kawada, K.; Sugita, K.; Ohtani, M.
Highly selective and orally active inhibitors of type IV collagenase (MMP-9 and MMP-2): N-sulfonylamino acid derivatives
J. Med. Chem.
41
640-649
1998
Homo sapiens
Manually annotated by BRENDA team
Cheng, D.; Shen, Q.; Nan, F.; Qian, Z.; Ye, Q.Z.
Purification and characterization of catalytic domains of gelatinase A with or without fibronectin insert for high-throughput inhibitor screening
Protein Expr. Purif.
27
63-74
2003
Homo sapiens
Manually annotated by BRENDA team
Briknarova, K.; Grishaev, A.; Banyai, L.; Tordai, H.; Patthy, L.; Llinas, M.
The second type II module from human matrix metalloproteinase 2: structure, function and dynamics
Structure
7
1235-1245
1999
Homo sapiens
Manually annotated by BRENDA team
Xu, X.; Chen, Z.; Wang, Y.; Yamada, Y.; Steffensen, B.
Functional basis for the overlap in ligand interactions and substrate specificities of matrix metalloproteinases-9 and -2
Biochem. J.
392
127-134
2005
Homo sapiens
Manually annotated by BRENDA team
Rossello, A.; Nuti, E.; Orlandini, E.; Carelli, P.; Rapposelli, S.; Macchia, M.; Minutolo, F.; Carbonaro, L.; Albini, A.; Benelli, R.; Cercignani, G.; Murphy, G.; Balsamo, A.
New N-arylsulfonyl-N-alkoxyaminoacetohydroxamic acids as selective inhibitors of gelatinase A (MMP-2)
Bioorg. Med. Chem.
12
2441-2450
2004
Homo sapiens
Manually annotated by BRENDA team
Kozaci, L.D.; Guner, A.; Oktay, G.; Guner, G.
Alterations in biochemical components of extracellular matrix in intervertebral disc herniation: role of MMP-2 and TIMP-2 in type II collagen loss
Cell Biochem. Funct.
24
431-436
2006
Homo sapiens
Manually annotated by BRENDA team
Di Carlo, A.; Terracciano, D.; Mariano, A.; Macchia, V.
Matrix metalloproteinase-2 and matrix metalloproteinase-9 type IV collagenases in serum of patients with pleural effusions
Int. J. Oncol.
26
1363-1368
2005
Homo sapiens
Manually annotated by BRENDA team
Khorramizadeh, M.R.; Aalizadeh, N.; Pezeshki, M.; Ghahary, A.; Zeraati, H.; Berahmeh, A.; Safa, O.; Saadat, F.
Determination of gelatinase A using a modified indirect hemagglutination assay in human prostate cancer screening and assessment of its correlation with prostate-specific antigen parameters
Int. J. Urol.
12
637-643
2005
Homo sapiens
Manually annotated by BRENDA team
Tam, E.M.; Moore, T.R.; Butler, G.S.; Overall, C.M.
Characterization of the distinct collagen binding, helicase and cleavage mechanisms of matrix metalloproteinase 2 and 14 (gelatinase A and MT1-MMP): the differential roles of the MMP hemopexin c domains and the MMP-2 fibronectin type II modules in collage
J. Biol. Chem.
279
43336-43344
2004
Homo sapiens
Manually annotated by BRENDA team
Gehrmann, M.L.; Douglas, J.T.; Banyai, L.; Tordai, H.; Patthy, L.; Llinas, M.
Modular autonomy, ligand specificity, and functional cooperativity of the three in-tandem fibronectin type II repeats from human matrix metalloproteinase 2
J. Biol. Chem.
279
46921-46929
2004
Homo sapiens
Manually annotated by BRENDA team
Kato, K.; Hara, A.; Kuno, T.; Kitaori, N.; Huilan, Z.; Mori, H.; Toida, M.; Shibata, T.
Matrix metalloproteinases 2 and 9 in oral squamous cell carcinomas: manifestation and localization of their activity
J. Cancer Res. Clin. Oncol.
131
340-346
2005
Homo sapiens
Manually annotated by BRENDA team
Ikejiri, M.; Bernardo, M.M.; Meroueh, S.O.; Brown, S.; Chang, M.; Fridman, R.; Mobashery, S.
Design, synthesis, and evaluation of a mechanism-based inhibitor for gelatinase A
J. Org. Chem.
70
5709-5712
2005
Homo sapiens
Manually annotated by BRENDA team
Xu, X.; Wang, Y.; Lauer-Fields, J.L.; Fields, G.B.; Steffensen, B.
Contributions of the MMP-2 collagen binding domain to gelatin cleavage. Substrate binding via the collagen binding domain is required for hydrolysis of gelatin but not short peptides
Matrix Biol.
23
171-181
2004
Homo sapiens
Manually annotated by BRENDA team
Di Carlo, A.; Terracciano, D.; Mariano, A.; Macchia, V.
Urinary gelatinase activities (matrix metalloproteinases 2 and 9) in human bladder tumors
Oncol. Rep.
15
1321-1326
2006
Homo sapiens
Manually annotated by BRENDA team
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
Biochem. J.
402
503-513
2007
Homo sapiens
Manually annotated by BRENDA team
Xu, X.; Chen, Z.; Wang, Y.; Bonewald, L.; Steffensen, B.
Inhibition of MMP-2 gelatinolysis by targeting exodomain-substrate interactions
Biochem. J.
406
147-155
2007
Homo sapiens
Manually annotated by BRENDA team
Moroy, G.; Denhez, C.; El Mourabit, H.; Toribio, A.; Dassonville, A.; Decarme, M.; Renault, J.H.; Mirand, C.; Bellon, G.; Sapi, J.; Alix, A.J.; Hornebeck, W.; Bourguet, E.
Simultaneous presence of unsaturation and long alkyl chain at P1 of Ilomastat confers selectivity for gelatinase A (MMP-2) over gelatinase B (MMP-9) inhibition as shown by molecular modelling studies
Bioorg. Med. Chem.
15
4753-4766
2007
Homo sapiens
Manually annotated by BRENDA team
Falcinelli, E.; Giannini, S.; Boschetti, E.; Gresele, P.
Platelets release active matrix metalloproteinase-2 in vivo in humans at a site of vascular injury: lack of inhibition by aspirin
Br. J. Haematol.
138
221-230
2007
Homo sapiens
Manually annotated by BRENDA team
Emara, M.; Cheung, P.Y.
Inhibition of sulfur compounds and antioxidants on MMP-2 and -9 at the activity level found during neonatal hypoxia-reoxygenation
Eur. J. Pharmacol.
544
168-173
2006
Homo sapiens, Sus scrofa
Manually annotated by BRENDA team
Hwang, E.S.; Lee, H.J.
Allyl isothiocyanate and its N-acetylcysteine conjugate suppress metastasis via inhibition of invasion, migration, and matrix metalloproteinase-2/-9 activities in SK-Hep 1 human hepatoma cells
Exp. Biol. Med. (Maywood)
231
421-430
2006
Homo sapiens
Manually annotated by BRENDA team
Sariahmetoglu, M.; Crawford, B.D.; Leon, H.; Sawicka, J.; Li, L.; Ballermann, B.J.; Holmes, C.; Berthiaume, L.G.; Holt, A.; Sawicki, G.; Schulz, R.
Regulation of matrix metalloproteinase-2 (MMP-2) activity by phosphorylation
FASEB J.
21
2486-2495
2007
Homo sapiens (P08253)
Manually annotated by BRENDA team
Kim, M.M.; Kim, S.K.
Chitooligosaccharides inhibit activation and expression of matrix metalloproteinase-2 in human dermal fibroblasts
FEBS Lett.
580
2661-2666
2006
Homo sapiens
Manually annotated by BRENDA team
Bogusiewicz, M.; Stryjecka-Zimmer, M.; Postawski, K.; Jakimiuk, A.J.; Rechberger, T.
Activity of matrix metalloproteinase-2 and -9 and contents of their tissue inhibitors in uterine leiomyoma and corresponding myometrium
Gynecol. Endocrinol.
23
541-546
2007
Homo sapiens
Manually annotated by BRENDA team
Strek, M.; Gorlach, S.; Podsedek, A.; Sosnowska, D.; Koziolkiewicz, M.; Hrabec, Z.; Hrabec, E.
Procyanidin oligomers from Japanese quince (Chaenomeles japonica) fruit inhibit activity of MMP-2 and MMP-9 metalloproteinases
J. Agric. Food Chem.
55
6447-6452
2007
Homo sapiens
Manually annotated by BRENDA team
Higashi, S.; Miyazaki, K.
Identification of amino acid residues of the matrix metalloproteinase-2 essential for its selective inhibition by beta-amyloid precursor protein-derived inhibitor
J. Biol. Chem.
283
10068-10078
2008
Homo sapiens
Manually annotated by BRENDA team
Mazzoni, A.; Mannello, F.; Tay, F.R.; Tonti, G.A.; Papa, S.; Mazzotti, G.; Di Lenarda, R.; Pashley, D.H.; Breschi, L.
Zymographic analysis and characterization of MMP-2 and -9 forms in human sound dentin
J. Dent. Res.
86
436-440
2007
Homo sapiens
Manually annotated by BRENDA team
Gao, L.; Kang, L.; Chen, Q.; Chen, C.; Xu, B.; Jiang, S.
Advanced glycation end products inhibit production and activity of matrix metalloproteinase-2 in human umbilical vein endothelial cells
J. Int. Med. Res.
35
709-715
2007
Homo sapiens
Manually annotated by BRENDA team
Rutges, J.; Kummer, J.; Oner, F.; Verbout, A.; Castelein, R.; Roestenburg, H.; Dhert, W.; Creemers, L.
Increased MMP-2 activity during intervertebral disc degeneration is correlated to MMP-14 levels
J. Pathol.
214
523-530
2008
Homo sapiens
Manually annotated by BRENDA team
Robinet, A.; Emonard, H.; Banyai, L.; Laronze, J.Y.; Patthy, L.; Hornebeck, W.; Bellon, G.
Collagen-binding domains of gelatinase A and thrombospondin-derived peptides impede endocytic clearance of active gelatinase A and promote HT1080 fibrosarcoma cell invasion
Life Sci.
82
376-382
2008
Homo sapiens
Manually annotated by BRENDA team
Whitlock, G.A.; Dack. K.N.; Dickinson, R.P.; Lewis M.L
A novel series of highly selective inhibitors of MMP-3
Bioorg. Med. Chem. Lett.
17
6750-6753
2007
Homo sapiens
Manually annotated by BRENDA team
Tao, P.; Fisher, J.F.; Shi, Q.; Vreven, T.; Mobashery, S.; Schlegel, H.B.
Matrix metalloproteinase 2 inhibition: combined quantum mechanics and molecular mechanics studies of the inhibition mechanism of (4-phenoxyphenylsulfonyl)methylthiirane and its oxirane analogue
Biochemistry
48
9839-9847
2009
Homo sapiens
Manually annotated by BRENDA team
Lisboa, R.A.; Lisboa, F.A.; de Castro Santos, G.; Andrade, M.V.; Cunha-Melo, J.R.
Matrix metalloproteinase 2 activity decreases in human periodontal ligament fibroblast cultures submitted to simulated orthodontic force
In Vitro Cell. Dev. Biol. Anim.
45
614-621
2009
Homo sapiens
Manually annotated by BRENDA team
Sato, Y.; Kishi, J.; Suzuki, K.; Nakamura, H.; Hayakawa, T.
Sonic extracts from a bacterium related to periapical disease activate gelatinase A and inactivate tissue inhibitor of metalloproteinases TIMP-1 and TIMP-2
Int. Endod. J.
42
1104-1111
2009
Homo sapiens
Manually annotated by BRENDA team
Momi, S.; Falcinelli, E.; Giannini, S.; Ruggeri, L.; Cecchetti, L.; Corazzi, T.; Libert, C.; Gresele, P.
Loss of matrix metalloproteinase 2 in platelets reduces arterial thrombosis in vivo
J. Exp. Med.
206
2365-2379
2009
Homo sapiens
Manually annotated by BRENDA team
Marquez-Aguirre, A.; Sandoval-Rodriguez, A.; Gonzalez-Cuevas, J.; Bueno-Topete, M.; Navarro-Partida, J.; Arellano-Olivera, I.; Lucano-Landeros, S.; Armendariz-Borunda, J.
Adenoviral delivery of dominant-negative transforming growth factor beta type II receptor up-regulates transcriptional repressor SKI-like oncogene, decreases matrix metalloproteinase 2 in hepatic stellate cell and prevents liver fibrosis in rats
J. Gene Med.
11
207-219
2009
Homo sapiens
Manually annotated by BRENDA team
Akers, W.J.; Xu, B.; Lee, H.; Sudlow, G.; Fields, G.B.; Achilefu, S.; Edwards, W.B.
Detection of MMP-2 and MMP-9 activity in vivo with a triple-helical peptide optical probe
Bioconjug. Chem.
23
656-663
2012
Homo sapiens
Manually annotated by BRENDA team
Koo, B.H.; Han, J.H.; Yeom, Y.I.; Kim, D.S.
Thrombin-dependent MMP-2 activity is regulated by heparan sulfate
J. Biol. Chem.
285
41270-41279
2010
Homo sapiens
Manually annotated by BRENDA team
Zhang, R.; Pan, X.; Huang, Z.; Weber, G.F.; Zhang, G.
Osteopontin enhances the expression and activity of MMP-2 via the SDF-1/CXCR4 axis in hepatocellular carcinoma cell lines
PLoS ONE
6
e23831
2011
Homo sapiens
Manually annotated by BRENDA team
Diaz, N.; Suarez, D.; Suarez, E.
Kinetic and binding effects in peptide substrate selectivity of matrix metalloproteinase-2: molecular dynamics and QM/MM calculations
Proteins
78
1-11
2010
Homo sapiens
Manually annotated by BRENDA team
Kawagoe, M.; Tsuruga, E.; Oka, K.; Sawa, Y.; Ishikawa, H.
Matrix metalloproteinase-2 degrades fibrillin-1 and fibrillin-2 of oxytalan fibers in the human eye and periodontal ligaments in vitro
Acta Histochem. Cytochem.
46
153-159
2013
Homo sapiens (P08253), Homo sapiens
Manually annotated by BRENDA team
Musumeci, G.; Magro, G.; Cardile, V.; Coco, M.; Marzagalli, R.; Castrogiovanni, P.; Imbesi, R.; Graziano, A.; Barone, F.; Di Rosa, M.; Castorina, S.; Castorina, A.
Characterization of matrix metalloproteinase-2 and -9, ADAM-10 and N-cadherin expression in human glioblastoma multiforme
Cell Tissue Res.
362
45-60
2015
Homo sapiens (P08253), Homo sapiens
Manually annotated by BRENDA team
Koo, B.; Kim, Y.; Han, J.; Kim, D.
Dimerization of matrix metalloproteinase-2 (MMP-2): functional implication in MMP-2 activation
J. Biol. Chem.
287
22643-22653
2012
Homo sapiens (P08253)
Manually annotated by BRENDA team
Higashi, S.; Hirose, T.; Takeuchi, T.; Miyazaki, K.
Molecular design of a highly selective and strong protein inhibitor against matrix metalloproteinase-2 (MMP-2)
J. Biol. Chem.
288
9066-9076
2013
Homo sapiens (P08253)
Manually annotated by BRENDA team
Goncalves, A.; Meschiari, C.; Stetler-Stevenson, W.; Nonato, M.; Alves, C.; Espreafico, E.; Gerlach, R.
Expression of soluble and functional full-length human matrix metalloproteinase-2 in Escherichia coli
J. Biotechnol.
157
20-24
2012
Homo sapiens (P08253), Homo sapiens
Manually annotated by BRENDA team
Ren, X.; Lamb, G.D.; Murphy, R.M.
Distribution and activation of matrix metalloproteinase-2 in skeletal muscle fibers
Am. J. Physiol. Cell Physiol.
317
C613-C625
2019
Homo sapiens (P08253), Homo sapiens, Rattus norvegicus (P33436)
Manually annotated by BRENDA team
Nejima, D.; Zarkouna, Y.; Pujol, P.; Gammoudi, A.; Boussen, H.; Manai, M.
Clinicopathologic and prognostic significance of gelatinase A in Tunisian colorectal cancer a case-control study
Appl. Immunohistochem. Mol. Morphol.
25
64-70
2017
Homo sapiens (P08253), Homo sapiens
Manually annotated by BRENDA team
Henriet, P.; Emonard, H.
Matrix metalloproteinase-2 not (just) a hero of the past
Biochimie
166
223-232
2019
Homo sapiens (P08253)
Manually annotated by BRENDA team
Nishihama, K.; Yasuma, T.; Yano, Y.; D Alessandro-Gabazza, C.N.; Toda, M.; Hinneh, J.A.; Baffour Tonto, P.; Takeshita, A.; Totoki, T.; Mifuji-Moroka, R.; Kobayashi, T.; Iwasa, M.; Takei, Y.; Morser, J.; Cann, I.; Gabazza, E.C.
Anti-apoptotic activity of human matrix metalloproteinase-2 attenuates diabetes mellitus
Metab. Clin. Exp.
82
88-99
2018
Homo sapiens (P08253), Homo sapiens
Manually annotated by BRENDA team
Baez, I.B.; Sampieri, C.L.; Solano, F.C.; Martinez Cazares, M.T.; Montero, H.; Cuevas, R.Z.
Activity of matrix metalloproteinase 2 and 9 isoforms in sputum samples from individuals infected with M. tuberculosis
Microb. Pathog.
135
103607
2019
Homo sapiens (P08253), Homo sapiens
Manually annotated by BRENDA team
Abu Bakar, A.R.; Ripen, A.M.; Merican, A.F.; Mohamad, S.B.
Enzymatic inhibitory activity of Ficus deltoidea leaf extract on matrix metalloproteinase-2, 8 and 9
Nat. Prod. Res.
33
1765-1768
2019
Homo sapiens (P08253)
Manually annotated by BRENDA team
Jana, S.; Chatterjee, K.; Ray, A.K.; DasMahapatra, P.; Swarnakar, S.
Regulation of matrix metalloproteinase-2 activity by COX-2-PGE2-pAKT axis promotes angiogenesis in endometriosis
PLoS ONE
11
e0163540
2016
Homo sapiens (P08253), Homo sapiens
Manually annotated by BRENDA team
Nicolai, E.; Sinibaldi, F.; Sannino, G.; Lagana, G.; Basoli, F.; Licoccia, S.; Cozza, P.; Santucci, R.; Piro, M.C.
Omega-3 and omega-6 fatty acids act as inhibitors of the matrix metalloproteinase-2 and matrix metalloproteinase-9 activity
Protein J.
36
278-285
2017
Homo sapiens (P08253)
Manually annotated by BRENDA team