Information on EC 3.4.24.24 - gelatinase A

New: Word Map on EC 3.4.24.24
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Mark a special word or phrase in this record:
Search Reference ID:
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


The expected taxonomic range for this enzyme is: Euteleostomi

EC NUMBER
COMMENTARY hide
3.4.24.24
-
RECOMMENDED NAME
GeneOntology No.
gelatinase A
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
Cleavage of gelatin type I and collagen types IV, V, VII, X. Cleaves the collagen-like sequence Pro-Gln-Gly-/-Ile-Ala-Gly-Gln
show the reaction diagram
cleaves the collagen-like sequence Pro-Gln-Gly-+-Ile-Ala-Gly-Gln, the term -+- depicts the point of cleavage
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
146480-35-5
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
gene MMP-2
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Mus musculus Nude BALB/c
gene Mmp2
UniProt
Manually annotated by BRENDA team
male
-
-
Manually annotated by BRENDA team
newborn undergoing hypoxia and reoxygenation
-
-
Manually annotated by BRENDA team
synthetic construct
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
physiological function
additional information
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-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-L-Pro-L-Gln-Gly-L-Ile-L-Ala-Gly-L-Gln-D-Arg + H2O
?
show the reaction diagram
-
-
-
-
?
2,4-Dinitrophenyl-Pro-Leu-Gly-Leu-Trp-Ala-D-Ala-NH2 + H2O
?
show the reaction diagram
-
-
-
-
-
7-amindo-4-methylcoumaryl--Pro-Leu-Gly-Leu-DPA-Ala-Arg-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
collagen type V + 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
-
-
-
?
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
-
-
?
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
gelatin type I + H2O
?
show the reaction diagram
-
-
-
-
?
gelatin type IV + H2O
?
show the reaction diagram
-
-
-
-
?
gelatin type V + 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 C15 + H2O
?
show the reaction diagram
-
non-selective peptide substrate
-
?
peptide C9 + H2O
?
show the reaction diagram
peptide C9R + H2O
?
show the reaction diagram
-
-
-
?
peptide m1A11 + H2O
?
show the reaction diagram
-
non-selective peptide substrate
-
?
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
-
-
-
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
Collagen + H2O
?
show the reaction diagram
-
-
-
-
?
collagen type IV + H2O
?
show the reaction diagram
-
-
-
-
?
collagene type IV + H2O
?
show the reaction diagram
-
-
-
-
?
extracellular matrix components + H2O
?
show the reaction diagram
-
-
-
?
Fibrinogen + H2O
?
show the reaction diagram
-
-
-
-
?
Gelatin + H2O
?
show the reaction diagram
Type I collagen + H2O
?
show the reaction diagram
M4VLM9
degradation
-
-
?
Type IV collagen + H2O
?
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ba2+
activates
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
additional information
no or poor activation by Zn2+, Mn2+, Mg2+, Cu2+, Fe2+, or Co2+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(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-(4-phenoxphenylsulfonyl)butane-1,2-dithiol
-
-
4-Aminobenzoyl-Gly-Pro-D-Leu-D-Ala-NHOH
-
-
5-(4-phenoxphenylsulfonyl)pentane-1,2-dithiol
-
-
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
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
ascorbic acid
-
-
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
curcumin
-
treatment of whole cell, significant inhibition of enzyme activity after 15 days with concomitant decrease in expression of membrane type-1 matrix metalloproteinase and focal adhesion kinase to almost background level
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
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-(R)-(2-(hydroxaminocarbonyl)methyl)-4-methylpentanoyl-L-naphthylalanyl-L-alanine-2-aminoethyl amide
-
TAPI-1
-
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
-
tissue inhibitors of metalloproteinase 2
-
TIMP2
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
interleukin 1beta
-
increases enzyme expression and activity in cardiac microvascular endothelial cells, involvement of PKC and/or MAPK signaling cascades, overview, the activation is inhibited by 52% by G6976, a PKC inhibitor, at 100 nM, while inhibitors SN50 and SP600125 have no effect on the activation
-
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
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, 30C
-
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, 37C
-
0.0172
fTHP-3
-
pH 7.5, 30C
-
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 - 2.5
peptide A13
0.4
peptide A13P
-
pH 7.5, 37C
-
0.1 - 0.4
peptide A13R
7.7
peptide A21
-
pH 7.5, 37C
-
3.2
peptide A21A
-
pH 7.5, 37C
-
1.2 - 3.6
peptide A3
2.2 - 4.3
peptide A34
2.4
peptide B37
-
pH 7.5, 37C
-
4.5
peptide B49
-
pH 7.5, 37C
-
0.2 - 2.2
peptide B74
0.6
peptide B74P
-
pH 7.5, 37C
-
0.8
peptide B74R
-
pH 7.5, 37C
-
0.9 - 4.4
peptide C9
6.4
peptide C9R
-
pH 7.5, 37C
-
0.0085
type I collagen
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
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
Homo sapiens
-
-
0.0616
alpha1(V)436-447 fTHP
Homo sapiens
-
pH 7.5, 30C
-
0.0045
collagen I
Gallus gallus
-
-
-
4.7 - 5.4
Dnp-Pro-beta-cyclohexyl-Ala-Gly-Cys(Me)-His-Ala-Lys(N-Me-Abz)-NH2
36.4
fibrinogen
Homo sapiens
-
cleavage of the alpha-chain of the native substrate, full-length MMP-2, pH 7.1, 37C
-
0.017
fTHP-3
Homo sapiens
-
30C
-
2.69
Gly-Pro-Gln-Gly-Ile-Ala-Gly-Gln
Homo sapiens
-
-
2
Gly-Pro-Gln-Gly-Ile-Ala-Ser-Gln
Homo sapiens
-
-
3.33
Gly-Pro-Gln-Gly-Ile-Phe-Gly-Gln
Homo sapiens
-
-
0.612
Gly-Pro-Gln-Gly-Ile-Trp-Gly-Gln
Homo sapiens
-
-
0.6 - 1.7
Mca-Pro-Leu-Gly-Leu-Dap-Ala-Arg-NH2
1.3 - 6
MOAcPLGLA2pr(Dnp)-AR-NH2
31 - 105
peptide A13
204
peptide A13P
Homo sapiens
-
pH7.5, 37C
-
2 - 18
peptide A13R
124
peptide A21
Homo sapiens
-
pH7.5, 37C
-
601
peptide A21A
Homo sapiens
-
pH7.5, 37C
-
73 - 400
peptide A3
60 - 202
peptide A34
353
peptide B37
Homo sapiens
-
pH7.5, 37C
-
510
peptide B49
Homo sapiens
-
pH7.5, 37C
-
17 - 622
peptide B74
264
peptide B74P
Homo sapiens
-
pH7.5, 37C
-
61
peptide B74R
Homo sapiens
-
pH7.5, 37C
-
26 - 740
peptide C9
0.0045
type I collagen
Homo sapiens
-
pH 7.5, 25C
-
0.0022
type V collagen
Homo sapiens
-
pH 7.5, 32C
-
0.00167
vitronectin of MW 65000 and 75000
Homo sapiens
-
-
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
30000
LS276-THP
Homo sapiens
-
pH 7.4, 37C
168026
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00046
2-(4-(4-[(2-thiiranylpropyl)sulfonyl]phenoxy)phenyl)acetic acid
-
-
0.00000000068
APP-IP-TIMP-2
-
pH 7.5, 37C
0.00005
methyl 2-(4-(4-[(2-thiiranylpropyl)-sulfonyl]phenoxy)phenyl)acetate
-
-
0.0000097
TIMP-1
-
pH 8.0, 25C, 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, 37C, 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
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, 22C
-
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
1045
-
37C
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5 - 7.6
-
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 - 9.3
-
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
7 - 9
activity range
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
-
assay at
40
recombinant enzyme
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 45
activity range
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.64
-
2D electrophoresis
6.2 - 6.4
-
isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
endplate; low content
Manually annotated by BRENDA team
-
aged arterial wall, colocalization of activated enzyme and transforming growth factor TGF-beta1. Treatment of young aortic rings with activated enzyme enhances active transforming growth factor TGF-beta-1, collagen, and fibronectin expression to the level of untreated old counterparts
Manually annotated by BRENDA team
-
melanoma cell
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
-
oxytalan fibers
Manually annotated by BRENDA team
-
tumor periphery
Manually annotated by BRENDA team
-
induced by acetic acid injection
Manually annotated by BRENDA team
-
high expression level of MMP-2 increasing during growth
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
-
GelA is expressed in fibroblasts surrounding apoptotic cells, expression of GelA is downregulated in the intestine by the end of metamorphosis when the tail is completely resorbed, and the adult intestine has formed
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
high activity
Manually annotated by BRENDA team
-
derived from premenopausal women aged 45-55 years who underwent total abdominal hysterectomy
Manually annotated by BRENDA team
-
regional lymph node invasion and distant metastases are more frequently observed in the MMP-2 positive cases, the MMP-2/TIMP-2 ratio is also positively correlated with MMP-2 activity, overview
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
-
male and female
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
GelA is expressed in fibroblasts surrounding apoptotic cells, spatial localization of MT1-MMP and GelA mRNAs in the tail during natural metamorphosis, overview
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
-
complex formed by MT1-MMP, TIMP-2
Manually annotated by BRENDA team
-
main localization in invertebral disc, immunohistochemic analysis, overview
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
68000
-
proMMP-2, SDS-PAGE
SUBUNITS
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
-
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60.8
-
Tm
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
stable in aqueous solution
-
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
as an inactive zymogen, rapid activation by 4-aminophenylmercuric acetate
-
catalytic domain
-
catalytic domain of mutated enzyme
-
col-1 module
-
from pulmonary artery smooth muscle plasma membrane
-
native MMP-2 from dentin inculding serial dilutions, method development
-
native, extracellular, inhibitor-free enzyme from glioblastoma cell line T98G cell culture medium
-
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 enzyme from HeLa S3 cells, native enzyme purified from HT-1080 cells
-
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
-
recombinant soluble enzyme from Escherichia coli cell-free extract by gelatin affinity chromatography
-
renaturation of recombinant MMP-2 in truncated form from Escherichia coli strain BL21(DE3) inclusion bodies after nickel affinity chromatography
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 cloned and expressed in Escherichia coli JM-109
-
cDNA of the mutated enzyme used to transfect HEK 293 cells
-
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
-
gene MMP-2 , cloning from skeletal muscle, DNA and amino acid sequence determination and analysis, sequence comparissons, expression of recombinant His-tagged MMP-2 in truncated form in Escherichia coli inclusion bodies
gene MMP-2, quantitative real time PCR expression analysis in glioblastoma
-
MMP-2 expression analysis in embryonic tissues of wild-type and caireticulin-deficient mice, overview
-
MMP-2 expression analysis in SK-Hep1 hepatoma cells, overview
-
pro-gelatinase A in transfected mammalian cell lines
-
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
-
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
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
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A404E
-
inactive
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
D49A
-
site-directed mutagenesis
E412D
-
site-directed mutagenesis
K50G
-
site-directed mutagenesis
K50R
-
site-directed mutagenesis
R19L
-
site-directed mutagenesis
R19L/R38L
-
site-directed mutagenesis
R38L
-
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
Y25A
-
site-directed mutagenesis
Y37A
-
site-directed mutagenesis
Y46A
-
site-directed mutagenesis
Y52A
-
site-directed mutagenesis
additional information
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
-
renaturation of recombinant MMP-2 in truncated form from Escherichia coli strain BL21(DE3) inclusion bodies after nickel affinity chromatography
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
diagnostics
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
Show Disease (8269 entries)
Longer loading times are possible.