Information on EC 3.4.24.24 - gelatinase A

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The expected taxonomic range for this enzyme is: Tetrapoda

EC NUMBER
COMMENTARY
3.4.24.24
-
RECOMMENDED NAME
GeneOntology No.
gelatinase A
REACTION
REACTION DIAGRAM
COMMENTARY
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
LITERATURE
hydrolysis of peptide bond
-
-
-
-
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
72 kDa Gelatinase
-
-
-
-
72 kDa Gelatinase type A
-
-
-
-
72 kDa type IV collagenase
-
-
72-kDa Gelatinase
-
-
-
-
72-kDa Gelatinase
-
-
Collagenase IV
-
-
-
-
Collagenase type IV
-
-
-
-
gelatinase A
-
-
human gelatinase A
-
-
human matrix metalloproteinase 2
-
-
human matrix metalloproteinase-2
-
-
matrix metalloprotease 2
-
-
Matrix metalloproteinase 2
-
-
-
-
Matrix metalloproteinase 2
-
-
matrix metalloproteinase-2
-
-
matrix metalloproteinase-2
P08253
-
matrix metalloproteinase-2
-
-
matrix metalloproteinase-2
-
-
matrix metalloprotenase-2
-
-
metalloproteinase-2
-
-
metrix metalloproteinase-2
-
-
MMP 2
-
-
-
-
MMP-2
-
-
MMP-2
P08253
-
MMP-2
-
-
MMP-2
Rattus norvegicus Wistar
-
-
-
MMP-2
-
-
MMP2
-
-
Type IV collagen metalloproteinase
-
-
-
-
Type IV collagenase
-
-
-
-
Type IV collagenase
-
-
Type IV collagenase/gelatinase
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
146480-35-5
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
expression in Escherichia coli
-
-
Manually annotated by BRENDA team
MMP-2 is a constitutive enzyme
-
-
Manually annotated by BRENDA team
patients with benign prostate hyperplasia or prostate cancer
-
-
Manually annotated by BRENDA team
patients with bladder cancer
-
-
Manually annotated by BRENDA team
patients with degenerative disc disease
-
-
Manually annotated by BRENDA team
patients with oral squamous cell carcinomas
-
-
Manually annotated by BRENDA team
patients with pleural effusions, such as malignant pleural effusion, breast carcinoma or lung carcinoma
-
-
Manually annotated by BRENDA team
recombinant enzyme
-
-
Manually annotated by BRENDA team
recombinant enzyme expressed in a Vaccinia virus-mammalian cell expression system
-
-
Manually annotated by BRENDA team
recombinant enzyme expressed in NSO mouse myeloma cells
-
-
Manually annotated by BRENDA team
recombinant wild-type from a myeloma cell expression system
-
-
Manually annotated by BRENDA team
synthetic gene in which two polypeptide fragments of the catalytic domain are joined with the deletion of the 19000 MW fibronectin-like insert of the catalytic domain, expressed in Escherichia coli
-
-
Manually annotated by BRENDA team
Fisher344 rats
-
-
Manually annotated by BRENDA team
Sprague-Dawley rats
-
-
Manually annotated by BRENDA team
Rattus norvegicus Wistar
male
-
-
Manually annotated by BRENDA team
newborn undergoing hypoxia and reoxygenation
-
-
Manually annotated by BRENDA team
synthetic construct
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
physiological function
-
in adult rats, in opposite to development of tooth, the MMP-9 and MMP-2 present in the odontogenic region does not seem to play a direct role in the remodeling matrix, even after post-shortening procedures which to lead an acceleration of the eruption process in the incisor
physiological function
Rattus norvegicus Wistar
-
in adult rats, in opposite to development of tooth, the MMP-9 and MMP-2 present in the odontogenic region does not seem to play a direct role in the remodeling matrix, even after post-shortening procedures which to lead an acceleration of the eruption process in the incisor
-
metabolism
-
evaluation of the effect that the hormonal fluctuations of the reproductive cycle have on the stromal remodeling and the expression and activity of matrix metalloproteinases MMP-2 and -9 in the adult female gerbil prostate, overview
additional information
-
the SDF-1a/CXCR4 axis is involved in osteopontininduced MMP-2 expression and activity, overview
additional information
-
thrombin-dependent MMP-2 activity is regulated by heparan sulfate, molecular mechanism, regulatory role of hemopexin-like domain in MMP-2 degradation, overview
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
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-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 + H2O
?
show the reaction diagram
-
-
-
?
Collagen + H2O
?
show the reaction diagram
-
-
-
-
?
Collagen + H2O
?
show the reaction diagram
-
type IV
-
-
-
Collagen + H2O
?
show the reaction diagram
-
type V
-
-
-
Collagen + H2O
?
show the reaction diagram
-
type V
-
-
-
Collagen + H2O
?
show the reaction diagram
-
type IV (to a lesser extent)
-
-
-
Collagen + H2O
?
show the reaction diagram
-
soluble triple helical type I collagen, 3/4- and 1/4-length collagen fragments are formed
-
-
-
Collagen + H2O
?
show the reaction diagram
-
binds type I collagen but does not cleave
-
-
-
Collagen + H2O
?
show the reaction diagram
-
fibrillar collagen, no cleavage of interstitial collagens
-
-
-
Collagen + H2O
?
show the reaction diagram
-
no cleavage of interstitial collagens
-
-
-
Collagen + H2O
?
show the reaction diagram
-
denatured collagen
-
-
-
Collagen + H2O
?
show the reaction diagram
-
several types
-
?
collagen type IV + H2O
?
show the reaction diagram
-
-
-
-
?
collagen type IV + H2O
?
show the reaction diagram
-
-
-
-
?
collagen type IV + H2O
?
show the reaction diagram
-
collagen zymography
-
-
?
collagen type V + H2O
?
show the reaction diagram
-
-
-
-
?
collagene type IV + H2O
?
show the reaction diagram
-
DQ-collagen type IV zymography
-
-
?
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
-
-
-
-
-
Elastin + H2O
?
show the reaction diagram
-
-
-
?
Elastin + H2O
?
show the reaction diagram
-
-
-
?
Elastin + H2O
?
show the reaction diagram
-
-
-
-
-
ephB1 + H2O
?
show the reaction diagram
-
-
-
?
ephB1 + H2O
?
show the reaction diagram
-
-
-
?
extracellular matrix components + H2O
?
show the reaction diagram
-
-
-
?
Fibrinogen + H2O
?
show the reaction diagram
-
-
-
-
?
Fibronectin + H2O
?
show the reaction diagram
-
-
-
-
-
Fibronectin + H2O
?
show the reaction diagram
-
-
-
?
Fibronectin + H2O
?
show the reaction diagram
-
-
-
?
Fibronectin + H2O
?
show the reaction diagram
-
-
-
?
Fibronectin + 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 + H2O
?
show the reaction diagram
-
-
-
-
-
Gelatin + H2O
?
show the reaction diagram
-
-
-
?
Gelatin + H2O
?
show the reaction diagram
-
-
-
?
Gelatin + H2O
?
show the reaction diagram
-
-
-
-
?
Gelatin + H2O
?
show the reaction diagram
-
-
-
-
-
Gelatin + H2O
?
show the reaction diagram
-
-
-
-
?
Gelatin + H2O
?
show the reaction diagram
P08253
-
-
-
?
Gelatin + H2O
?
show the reaction diagram
-
gelatin zymography
-
-
?
Gelatin + H2O
?
show the reaction diagram
-
gelatin zymography
-
-
?
Gelatin + H2O
?
show the reaction diagram
-
gelatin zymography
-
-
?
Gelatin + H2O
?
show the reaction diagram
-
gelatin zymography
-
-
?
Gelatin + H2O
?
show the reaction diagram
-
gelatin zymography
-
-
?
Gelatin + H2O
?
show the reaction diagram
-
gelatin zymography using porcine gelatin type A
-
-
?
Gelatin + H2O
?
show the reaction diagram
Rattus norvegicus Wistar
-
-
-
-
?
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
-
-
-
-
-
Laminin + H2O
?
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
-
-
-
-
-
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 A13 + H2O
?
show the reaction diagram
-
-
-
?
peptide A13P + H2O
?
show the reaction diagram
-
-
-
?
peptide A13R + 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 A3 + H2O
?
show the reaction diagram
-
-
-
?
peptide A34 + 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 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 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
-
-
-
MOAcPLGLA2pr(Dnp)-AR-NH2 + H2O
?
show the reaction diagram
-
fluorogenic quenching substrate
-
?
additional information
?
-
-
specificity: tolerates only small amino acids such as Gly and Ala in subsite P1, prefers hydrophobic, aliphatic residues in subsite P1'
-
-
-
additional information
?
-
-
laminin,native or denatured type I collagen, native or denatured types II, IV, V, and X collagen or the NC1 domain of type VII collagen, elastin,SPARC, tenascin and MatrigelTM are not bound by the recombinant C domain
-
?
additional information
?
-
-
Mca-Arg-Pro-Lys-Pro-Val-Glu-Nva-Trp-Arg-Lys(Dnp)-NH2 and DABCYL-Leu-Ala-Gln-Ala-Val-Arg-Ser-Ser-Ser-Arg-EDANS are no substrates
-
?
additional information
?
-
-
may be responsible for the pathological degradation and/or normal turnover of vitronectin
-
-
-
additional information
?
-
-
constitutively expressed in human rheumatoid synovial cells
-
-
-
additional information
?
-
-
activation of progelatinase B is mediated by gelatinase A species that may be localized in the surface of tumor cells and enhance matrix degradation during cancer metastasis
-
-
-
additional information
?
-
P08253
facilitates tmumor metastasis and angiogenesis by hydrolyzing components of the extracwllular matrix
-
?
additional information
?
-
-
implicated in tumor cell metastasis and angiogenesis
-
?
additional information
?
-
-
important role in extracellular matrix degradation during cell migration and tissue remodeling, involved in development, inflammation, wound healing, tumor invasion, metastasis and other physiological and pathological processes
-
?
additional information
?
-
-
important role in tumor angiogenesis
-
?
additional information
?
-
-
plays a key role in angiogenesis and tumor metastasis
-
?
additional information
?
-
-
collagen binding domain is absolutely required for enzyme-dependent cleavage of full-length collagen alpha-chain, but not for short protein fragments such as those generated by hydrolysis of gelatin
-
-
-
additional information
?
-
-
collagen binding domains of matrix metalloproteinases MMP-2 and MMP-9 bind the same or closely positioned sites on type I collagen
-
-
-
additional information
?
-
-
investigation of ligand binding properties of the three fibronectin type II repeats of enzyme using collagen mimic peptide (L-Pro-L-Pro-Gly)6 and propeptide segment PIIKFPGDVA. Each module interacts essentially as an autonomous unit with these peptides, but enzyme shows cooperative participation toward a closer mimic of collagen, ((Gly-L-Pro-L-Pro-)12)3 in triple helical configuration
-
-
-
additional information
?
-
-
activation of MMP-2 may contribute to dentin matrix degradation, which occurs during caries progression and follows rresin bonding. Inhibition of MMP-2 proteolytic activity may slow caries progression and increase the durability of resin-dentin bond, overview
-
-
-
additional information
?
-
-
Akt signaling is involved in the activation of MMP-2, and this Akt-induced activation of MMP-2 is responsible for reorganization of the actin cytoskeleton into a cortical pattern with parallel rounding of chondrogenic competent cells, MMP-2 regulation, not related to Erk signaling, overview
-
-
-
additional information
?
-
-
chitooligosaccharides may play an important role in the prevention and treatment of several MMP-2 mediated health problems such as metastasis and wrinkle formation, overview
-
-
-
additional information
?
-
-
intervertebral disc degeneration is associated with the increased expression of several matrix metalloproteinases, in particular MMP-2, overview
-
-
-
additional information
?
-
-
the enzyme degrades proteins of the extracellular matrix in the uterus and might be involved in the growth of leiomyoma and corresponding myometrium, overview
-
-
-
additional information
?
-
-
TSP-1 acts in LRP-mediated clearance of MMP-2, TIMP-2 complexing leads to MMP-2 accumulation in the cells
-
-
-
additional information
?
-
-
MMP-2 CBD-binding peptides from a random peptide library screening using biotinylated recombinant CBD domain, and interactions of immobilized synthetic peptides with the recombinant CBD, MMP-2E404A, MMP-2DELTACBD and AlkCBD, overview
-
-
-
additional information
?
-
-
the enzyme shows strong interaction with TSP-1 and CBD123, surface plasmon resonance analysis, overview
-
-
-
additional information
?
-
-
gel zymography for activity determination
-
-
-
additional information
?
-
-
kinetic and binding effects in peptide substrate selectivity of matrix metalloproteinase-2, molecular dynamics and QM/MM calculations, computational analysis of binding and hydrolysis reaction by MMP-2 of two peptide substrates selected by the enzyme from a phage peptide library, molecular dynamics simulations of the Michaelis complex, overview
-
-
-
additional information
?
-
-
MMP-2 shows gelatinolytic activity
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
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
-
-
-
-
?
Gelatin + H2O
?
show the reaction diagram
-
-
-
-
?
Gelatin + H2O
?
show the reaction diagram
-
-
-
-
?
Gelatin + H2O
?
show the reaction diagram
-
-
-
-
?
Gelatin + H2O
?
show the reaction diagram
P08253
-
-
-
?
Gelatin + H2O
?
show the reaction diagram
Rattus norvegicus Wistar
-
-
-
-
?
additional information
?
-
-
may be responsible for the pathological degradation and/or normal turnover of vitronectin
-
-
-
additional information
?
-
-
constitutively expressed in human rheumatoid synovial cells
-
-
-
additional information
?
-
-
activation of progelatinase B is mediated by gelatinase A species that may be localized in the surface of tumor cells and enhance matrix degradation during cancer metastasis
-
-
-
additional information
?
-
P08253
facilitates tmumor metastasis and angiogenesis by hydrolyzing components of the extracwllular matrix
-
?
additional information
?
-
-
implicated in tumor cell metastasis and angiogenesis
-
?
additional information
?
-
-
important role in extracellular matrix degradation during cell migration and tissue remodeling, involved in development, inflammation, wound healing, tumor invasion, metastasis and other physiological and pathological processes
-
?
additional information
?
-
-
important role in tumor angiogenesis
-
?
additional information
?
-
-
plays a key role in angiogenesis and tumor metastasis
-
?
additional information
?
-
-
collagen binding domain is absolutely required for enzyme-dependent cleavage of full-length collagen alpha-chain, but not for short protein fragments such as those generated by hydrolysis of gelatin
-
-
-
additional information
?
-
-
collagen binding domains of matrix metalloproteinases MMP-2 and MMP-9 bind the same or closely positioned sites on type I collagen
-
-
-
additional information
?
-
-
activation of MMP-2 may contribute to dentin matrix degradation, which occurs during caries progression and follows rresin bonding. Inhibition of MMP-2 proteolytic activity may slow caries progression and increase the durability of resin-dentin bond, overview
-
-
-
additional information
?
-
-
Akt signaling is involved in the activation of MMP-2, and this Akt-induced activation of MMP-2 is responsible for reorganization of the actin cytoskeleton into a cortical pattern with parallel rounding of chondrogenic competent cells, MMP-2 regulation, not related to Erk signaling, overview
-
-
-
additional information
?
-
-
chitooligosaccharides may play an important role in the prevention and treatment of several MMP-2 mediated health problems such as metastasis and wrinkle formation, overview
-
-
-
additional information
?
-
-
intervertebral disc degeneration is associated with the increased expression of several matrix metalloproteinases, in particular MMP-2, overview
-
-
-
additional information
?
-
-
the enzyme degrades proteins of the extracellular matrix in the uterus and might be involved in the growth of leiomyoma and corresponding myometrium, overview
-
-
-
additional information
?
-
-
TSP-1 acts in LRP-mediated clearance of MMP-2, TIMP-2 complexing leads to MMP-2 accumulation in the cells
-
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
-
required, gelatinase A synthetic 19000 MW catalytic domain
Ca2+
-
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
Ca2+
-
hemopexin-like domain requires Ca2+ for fibronectin and heparin binding
Ca2+
-
active site requires calcium ions
Ca2+
-
required, optimal concentration 10 mM
Ca2+
-
dependent on
Ca2+
-
required
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
Zn2+
-
required, gelatinase A synthetic 19000 MW catalytic domain, inhibition at high concentration
Zn2+
-
zinc-dependent
Zn2+
-
zinc-dependent metalloproteinase
Zn2+
-
structural zinc ion
Zn2+
-
zinc-dependent endopeptidase
Zn2+
-
zinc-dependent gelatinase
Zn2+
-
active site requires zinc ions
Zn2+
P08253
a zinc-endopeptidase
Zn2+
-
dependent on
Zn2+
-
required, metalloprotease
Zn2+
-
dependent on
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
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
-
-
1,10-phenanthroline
-
a non-specific inhibitor of metalloproteinases
1,10-phenanthroline
-
-
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
-
-
-
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%
EDTA
-
-
EGTA
-
-
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
-
-
ilomastat
-
a pan-MMP inhibitor, strong inhibition
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
-
synthetic decapeptide APP-IP(APP586-595)
ISYGNDALMP
-
APP-derived inhibitory peptide, APP-IP, selective inhibition of MMP-2, An MMP-2 mutant, with deleted hemopexin-like domain and three fibronectin-like type II domains, and native MMP-2 showed similar affinities for APP-IP, suggesting that only the catalytic domain of MMP-2 is essential for the interaction, mutational interaction analysis, overview, inhibition of recombinant wild-type enzyme and truncated enzyme mutants, overview
ISYGNDALMPSL
-
APP586-597
ISYGNDALMPSLTETK
-
APP586-601
L-ascorbic acid
-
-
L-cysteine
-
-
L-histidine
-
-
L-homocysteine
-
-
L-methionine
-
-
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
-
specific for MMP-2
-
TIMP-2
-
pro-MMP-2-TIMP-2 complexes are endocytosed into HT-1080 cells
-
TIMP-2
-
-
-
TIMP-4
-
tissue inhibitor of metalloproteinases
-
Tissue inhibitor of metalloproteinase-1
-
-
-
Tissue inhibitor of metalloproteinase-2
-
TIMP-2, not only a potent inhibitor of the activated enzyme but also prevents the generation of low-molecular-mass species and full enzymic activity from the zymogen
-
Tissue inhibitor of metalloproteinase-2
-
activity of the inhibitor is regulated by C-terminal domain interactions
-
Tissue inhibitor of metalloproteinase-2
-
purification and characterization of a two-chain form of the inhibitor and a low MW TIMP-like protein, proteolytic processing of TIMP-2 plays a role in the regulation of gelatinase A in the extracellular matrix
-
Tissue inhibitor of metalloproteinase-2
-
gelatinase A/TIMP-2-complex may be a matrix metalloproteinase of the second step: it starts its proteolytic attack after it has switched off the activity of other matrix metalloproteinases
-
Tissue inhibitor of metalloproteinase-2
-
-
-
Tissue inhibitor of metalloproteinase-2
-
-
-
Tissue inhibitor of metalloproteinases
-
-
-
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
methyl 2-(4-(4-[(2-thiiranylpropyl)-sulfonyl]phenoxy)phenyl)acetate
-
mechanism-based inhibitor, selective for enzyme
additional information
-
not: inhibitors of serine, cysteine or aspartic proteinases
-
additional information
-
dithiothreitol does not interfere with heparin binding
-
additional information
-
inhibition of MMP-2 gelatinolysis by targeting exodomain-substrate interactions
-
additional information
-
inhibitor synthesis and molecular docking, overview
-
additional information
-
inhibition potency of sulfur-containing compounds, overview
-
additional information
-
allyl isothiocyanate and N-acetylcysteinyl-allyl isothiocyanate downregulate MMP-2 expression in SK-Hep1 hepatoma cells, as well as adhesion, invasion, and migration, overview
-
additional information
-
CBD123 decreases active MMP-2 levels in HT-1080 cells, but only marginally the content of pro-MMP-2, overview
-
additional information
-
calreticulin-deficient null mice embryos show increased MMP-2 expression and activity, phosphatidylinositol 3 kinase inhibitor decreases the MMP-2 expression, overview
-
additional information
-
simultaneous binding of each ligand heparan sulfate and hirudin to the exosites is necessary for the complete inhibition of MMP-2 degradation by thrombin
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
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
-
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
-
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
-
additional information
-
no activation by endopeptidases (trypsin, chymotrypsin, plasmin, plasma kallikrein, thrombin, neutrophil elastase, cathepsin G, matrix metalloproteinase 3, thermolysin); rapid activation of the zymogen by 4-aminophenylmercuric acetate
-
additional information
-
rapid activation of the zymogen by 4-aminophenylmercuric acetate; trypsin is a poor activator
-
additional information
-
interaction of the zymogen with fetuin or asialofetuin results in cleavage to lower MW forms and activation
-
additional information
-
activation of pro-MMP-2 by 4-aminophenylmercuric acetate
-
additional information
-
implantation of 9L glioma cells into brain increases the expression of MMP-2, overview
-
additional information
-
a complex formed by MT1-MMP, TIMP-2, and MMP-2 and located at the cell surface, is involved in MMP-2 activation, overview
-
additional information
-
sonicated bacterial extract from Porphyromonas gingivalis (0.0001 mg/ml at 37C for 18 h) activates MMP-2
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.136
Ac-Pro-Leu-Gly-[2-mercapto-4-methylpentanoyl]-Leu-Gly-OEt
-
pH 7.5, 37C, GaCD, without fibronectin-like insert
0.172
Ac-Pro-Leu-Gly-[2-mercapto-4-methylpentanoyl]-Leu-Gly-OEt
-
pH 7.5, 37C, GaCDfn, with fibronectin-like insert
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
Dnp-Pro-beta-cyclohexyl-Ala-Gly-Cys(Me)-His-Ala-Lys(N-Me-Abz)-NH2
-
pH 7.5, 37C, GaCD, without fibronectin-like insert
0.118
Dnp-Pro-beta-cyclohexyl-Ala-Gly-Cys(Me)-His-Ala-Lys(N-Me-Abz)-NH2
-
pH 7.5, 37C, GaCDfn, with fibronectin-like insert
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
Mca-Pro-Leu-Gly-Leu-Dap-Ala-Arg-NH2
-
pH 7.5, 37C, GaCDfn, with fibronectin-like insert
0.0099
Mca-Pro-Leu-Gly-Leu-Dap-Ala-Arg-NH2
-
pH 7.5, 37C, GaCD, without fibronectin-like insert
0.00152
MOAcPLGLA2pr(Dnp)-AR-NH2
-
pH 8.0, 25C, 45 kDa form
1.3
peptide A13
-
pH 7.5, 37C
-
1.3
peptide A13
-
37C
-
2.5
peptide A13
-
37C, mutant E412D
-
0.4
peptide A13P
-
pH 7.5, 37C
-
0.1
peptide A13R
-
37C, mutant E412D
-
0.4
peptide A13R
-
pH 7.5, 37C
-
0.4
peptide A13R
-
37C
-
7.7
peptide A21
-
pH 7.5, 37C
-
3.2
peptide A21A
-
pH 7.5, 37C
-
1.2
peptide A3
-
37C, mutant E412D
-
3.6
peptide A3
-
pH 7.5, 37C
-
3.6
peptide A3
-
37C
-
2.2
peptide A34
-
pH 7.5, 37C
-
2.2
peptide A34
-
37C
-
4.3
peptide A34
-
37C, mutant E412D
-
2.4
peptide B37
-
pH 7.5, 37C
-
4.5
peptide B49
-
pH 7.5, 37C
-
0.2
peptide B74
-
37C, mutant E412D
-
2.2
peptide B74
-
pH 7.5, 37C
-
2.2
peptide B74
-
37C
-
0.6
peptide B74P
-
pH 7.5, 37C
-
0.8
peptide B74R
-
pH 7.5, 37C
-
0.9
peptide C9
-
37C, mutant E412D
-
4.4
peptide C9
-
pH 7.5, 37C
-
4.4
peptide C9
-
37C
-
6.4
peptide C9R
-
pH 7.5, 37C
-
0.0085
type I collagen
-
-
-
0.0085
type I collagen
-
pH 7.5, 25C
-
0.0012
vitronectin of MW 65000
-
-
-
0.001
vitronectin of MW 75000
-
-
-
0.00306
MOAcPLGLA2pr(Dnp)-AR-NH2
-
pH 8.0, 25C, 62 kDa form
additional information
additional information
-
kinetics of trunacted enzyme and modified fibrinogen substrates, Michaelis-Menten mechanism, overview
-
additional information
additional information
-
kinetic analysis of LS276-THP hydrolysis by MMP-2
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
16.7
Ac-Pro-Leu-Gly-[2-mercapto-4-methylpentanoyl]-Leu-Gly-OEt
-
pH 7.5, 37C, GaCD, without fibronectin-like insert
19.5
Ac-Pro-Leu-Gly-[2-mercapto-4-methylpentanoyl]-Leu-Gly-OEt
-
pH 7.5, 37C, GaCDfn, with fibronectin-like insert
1.6
Acetyl-Pro-Leu-Gly-thioester-Leu-Leu-Gly ethyl ester
-
-
0.0616
alpha1(V)436-447 fTHP
-
pH 7.5, 30C
-
0.0045
collagen I
-
-
-
4.7
Dnp-Pro-beta-cyclohexyl-Ala-Gly-Cys(Me)-His-Ala-Lys(N-Me-Abz)-NH2
-
pH 7.5, 37C, GaCDfn, with fibronectin-like insert
5.4
Dnp-Pro-beta-cyclohexyl-Ala-Gly-Cys(Me)-His-Ala-Lys(N-Me-Abz)-NH2
-
pH 7.5, 37C, GaCD, without fibronectin-like insert
36.4
Fibrinogen
-
cleavage of the alpha-chain of the native substrate, full-length MMP-2, pH 7.1, 37C
-
0.017
fTHP-3
-
30C
-
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
Mca-Pro-Leu-Gly-Leu-Dap-Ala-Arg-NH2
-
pH 7.5, 37C, GaCDfn, with fibronectin-like insert
1.7
Mca-Pro-Leu-Gly-Leu-Dap-Ala-Arg-NH2
-
pH 7.5, 37C, GaCD, without fibronectin-like insert
1.3
MOAcPLGLA2pr(Dnp)-AR-NH2
-
pH 8.0, 25C, 45 kDa form
3 - 6
MOAcPLGLA2pr(Dnp)-AR-NH2
-
pH 8.0, 25C, 62 kDa form
3.18
MOAcPLGLA2pr(Dnp)-AR-NH2
-
pH 8.0, 25C, 62 kDa form
31
peptide A13
-
37C, mutant E412D
-
105
peptide A13
-
pH7.5, 37C
-
105
peptide A13
-
37C
-
204
peptide A13P
-
pH7.5, 37C
-
2 - 8
peptide A13R
-
pH7.5, 37C
-
2 - 8
peptide A13R
-
37C
-
18
peptide A13R
-
37C, mutant E412D
-
124
peptide A21
-
pH7.5, 37C
-
601
peptide A21A
-
pH7.5, 37C
-
73
peptide A3
-
37C, mutant E412D
-
400
peptide A3
-
pH7.5, 37C
-
400
peptide A3
-
37C
-
60
peptide A34
-
37C, mutant E412D
-
202
peptide A34
-
pH7.5, 37C
-
202
peptide A34
-
37C
-
353
peptide B37
-
pH7.5, 37C
-
510
peptide B49
-
pH7.5, 37C
-
17
peptide B74
-
37C, mutant E412D
-
622
peptide B74
-
pH7.5, 37C
-
622
peptide B74
-
37C
-
264
peptide B74P
-
pH7.5, 37C
-
61
peptide B74R
-
pH7.5, 37C
-
26
peptide C9
-
37C, mutant E412D
-
740
peptide C9
-
pH7.5, 37C
-
740
peptide C9
-
37C
-
0.0045
type I collagen
-
pH 7.5, 25C
-
0.0022
type V collagen
-
pH 7.5, 32C
-
0.00167
vitronectin of MW 65000 and 75000
-
-
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
30000
LS276-THP
-
pH 7.4, 37C
0
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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, 25C, 62 kDa form
-
0.0000072
TIMP-2
-
pH 8.0, 25C, 62 kDa form
-
0.000275
TIMP-2
-
pH 8.0, 25C, 45 kDa form
-
0.0011
TIMP-2
-
pH 7.5, 25C
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00028
(2E)-3-(N-hydroxycarbamoyl)-2-(3-phenylpropylidene)propionyl-L-tryptophan-N-methylamide
-
-
0.000123
(2E)-3-(N-hydroxycarbamoyl)-2-heptylidenepropionyl-L-tryptophan-N-methylamide
-
-
0.0000092
(2E)-3-(N-hydroxycarbamoyl)-2-isopropionyl-L-tryptophan-N-methylamide
-
-
0.00012
(2E)-3-(N-hydroxycarbamoyl)-2-[(2E)-3-phenylprop-2-en-1-ylidene]propionyl-L-tryptophan-N-methylamide
-
-
0.0785
(2E)-3-(N-hydroxycarbamoyl)-2-[(2E)-but-2-en-1-ylidene]propionyl-L-tryptophan-N-methylamide
-
-
0.000188
2-([4-[3'-(2-aminoethoxy)-2-methylbiphenyl-4-yl]piperidin-1-yl]sulfonyl)-N-hydroxy-2-methylpropanamide
-
-
0.000009
2-[(4-biphenyl-4-yl-3,6-dihydropyridin-1(2H)-yl)sulfonyl]-N-hydroxyacetamide
-
-
0.000534
2-[(4-[3'-[2-(dimethylamino)ethoxy]-2-methylbiphenyl-4-yl]piperidin-1-yl)sulfonyl]-N-hydroxy-2-methylpropanamide
-
-
0.000776
2-[[4-(2,3'-dimethylbiphenyl-4-yl)-3,6-dihydropyridin-1(2H)-yl]sulfonyl]-N-hydroxyacetamide
-
-
0.00062
2-[[4-(2-chlorobiphenyl-4-yl)-3,6-dihydropyridin-1(2H)-yl]sulfonyl]-N-hydroxyacetamide
-
-
0.00438
2-[[4-(2-ethylbiphenyl-4-yl)-3,6-dihydropyridin-1(2H)-yl]sulfonyl]-N-hydroxyacetamide
-
-
0.000017
2-[[4-(2-fluorobiphenyl-4-yl)-3,6-dihydropyridin-1(2H)-yl]sulfonyl]-N-hydroxyacetamide
-
-
0.000998
2-[[4-(3'-ethoxy-2-methylbiphenyl-4-yl)-3,6-dihydropyridin-1(2H)-yl]sulfonyl]-N-hydroxyacetamide
-
-
0.000457
2-[[4-(3'-ethoxy-2-methylbiphenyl-4-yl)piperidin-1-yl]sulfonyl]-N-hydroxy-2-methylpropanamide
-
-
0.001208
2-[[4-(3'-ethyl-2-methylbiphenyl-4-yl)-3,6-dihydropyridin-1(2H)-yl]sulfonyl]-N-hydroxyacetamide
-
-
0.141
ascorbic acid
-
recombinant enzyme
0.195
GSH
-
recombinant enzyme
0.547
GSSG
-
recombinant enzyme
0.0000005
ilomastat
-
pH 7.4, 37C
0.0000011
ilomastat
-
-
0.0073 - 0.015
ISYGNDALMP
-
pH 7.5, 37C, recombinant fragments of MMP-2
0.061
L-cysteine
-
recombinant enzyme
0.118
L-histidine
-
recombinant enzyme
0.727
L-homocysteine
-
recombinant enzyme
1
N-acetylcysteine
-
recombinant enzyme
0.00308
N-hydroxy-2-([4-[2-(trifluoromethyl)biphenyl-4-yl]-3,6-dihydropyridin-1(2H)-yl]sulfonyl)acetamide
-
-
0.000173
N-hydroxy-2-([4-[2-methyl-3'-(trifluoromethoxy)biphenyl-4-yl]-3,6-dihydropyridin-1(2H)-yl]sulfonyl)acetamide
-
-
0.000262
N-hydroxy-2-([4-[3'-(2-hydroxyethoxy)-2-methylbiphenyl-4-yl]piperidin-1-yl]sulfonyl)-2-methylpropanamide
-
-
0.000853
N-hydroxy-2-([4-[3'-(2-methoxyethoxy)-2-methylbiphenyl-4-yl]piperidin-1-yl]sulfonyl)-2-methylpropanamide
-
-
0.000196
N-hydroxy-2-([4-[3'-(methoxymethyl)-2-methylbiphenyl-4-yl]-3,6-dihydropyridin-1(2H)-yl]sulfonyl)acetamide
-
-
0.000196
N-hydroxy-2-methyl-2-[(4-[2-methyl-3'-[2-(methylamino)ethoxy]biphenyl-4-yl]piperidin-1-yl)sulfonyl]propanamide
-
-
0.000529
N-hydroxy-2-[(4-[4-[6-(2-hydroxyethoxy)pyridin-2-yl]-3-methylphenyl]piperidin-1-yl)sulfonyl]-2-methylpropanamide
-
-
0.00032
N-hydroxy-2-[[4-(2-methylbiphenyl-4-yl)-3,6-dihydropyridin-1(2H)-yl]sulfonyl]acetamide
-
-
0.000222
N-hydroxy-2-[[4-(3'-methoxy-2-methylbiphenyl-4-yl)-3,6-dihydropyridin-1(2H)-yl]sulfonyl]acetamide
-
-
0.01
peptide P713
-
pH 7.0, 22C
-
0.0342
UK-370106
-
-
8.68
L-methionine
-
recombinant enzyme
additional information
additional information
-
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.368
-
GaCDfn, with fibronectin-like insert
11.8
-
GaCD, without fibronectin-like insert
1045
-
37C
additional information
-
-
additional information
-
-
additional information
-
assay procedure
additional information
-
quantitative MMP-2 expression analysis of untreated and induced cells, overview
additional information
-
-
additional information
-
enzyme activity in leiomyoma and myometrium, overview
additional information
-
MMP-2 activity in embryonic tissues of wild-type and caireticulin-deficient mice, overview
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7
-
acetyl-Pro-Leu-Gly-thioester-Leu-Leu-Gly ethyl ester, gelatinase A synthetic 19000 MW catalytic domain
7
-
assay at, fluorogenic peptide substrate
7.4
-
assay at
7.4
-
assay at
7.5 - 7.6
P08253
assay at
7.5
-
assay at
7.6
-
assay at, gelatin or collagen IV zymography
7.6
-
assay at
7.6
-
assay at
8
-
assay at
8.5
-
azocoll
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
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
-
-
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
LITERATURE
22
-
assay at
37
-
assay at
37
-
assay at
37
-
assay at
37
-
assay at
37
-
assay at
37
P08253
assay at
37
-
assay at
37
-
assay at
37
-
assay at
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.64
P08253
2D electrophoresis
6.2 - 6.4
-
isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
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
-
secretion of MMP-2
Manually annotated by BRENDA team
-
human platelets contain matrix metalloproteinase 2 and release it upon activation
Manually annotated by BRENDA team
-
low activity
Manually annotated by BRENDA team
-
expression analysis in brain after implantation of 9L glioma cells, overview
Manually annotated by BRENDA team
-
recombinant pro-MMP-2
Manually annotated by BRENDA team
-
from human rheumatoid synovial cells
Manually annotated by BRENDA team
-
from Rous-sarcoma virus-transformed chicken embryo fibroblasts
Manually annotated by BRENDA team
-
conditioned medium from T98G human glioblastoma cells
Manually annotated by BRENDA team
-
from H-ras-transformed human bronchial epithelial cells (TBE-1)
Manually annotated by BRENDA team
-
latent proenzyme
Manually annotated by BRENDA team
-
from HeLa cells co-infected with each of the recombinant Vaccinia viruses and with vTF7-3
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
-
GelA is expressed in fibroblasts surrounding apoptotic cells of intestine and tail
Manually annotated by BRENDA team
-
primary dermal
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
-
leukemia cell line, secretion of MMP-2
Manually annotated by BRENDA team
-
fibrosarcoma cell
Manually annotated by BRENDA team
-
tumour cells developed in mice, high expression level
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
-
cirrhotic liver
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
-
hepatoma cell line
Manually annotated by BRENDA team
-
pulmonary artery smooth muscle
Manually annotated by BRENDA team
-
vascular smooth muscle, colocalization of activated enzyme and transforming growth factor TGF-beta1. Treatment of vascular smooth muscle cells in vitro 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
-
tissue samples of oral squamous cell carcinomas
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
-
activity of MMP-2 in odontogenic region of the rat incisor tooth after post shortening procedure, overview
Manually annotated by BRENDA team
Rattus norvegicus Wistar
-
activity of MMP-2 in odontogenic region of the rat incisor tooth after post shortening procedure, overview
-
Manually annotated by BRENDA team
-
enzyme level and expression analysis in response to advanced glycation products
Manually annotated by BRENDA team
-
stimulated, release of MMP-2 in vitro
Manually annotated by BRENDA team
-
fibroids of different size show equal MMP-2 activity
Manually annotated by BRENDA team
additional information
-
co-localization of MT1-MMP and GelA mRNAs during amphibian development, overview
Manually annotated by BRENDA team
additional information
-
expression analysis of MMP-2 in dog tumor tissues, overview
Manually annotated by BRENDA team
additional information
-
MMP-2 activity in tissues taken from newborn piglets undergoing hypoxia and reoxygenation, overview
Manually annotated by BRENDA team
additional information
-
MMP-2 is increased in tumor cells
Manually annotated by BRENDA team
additional information
P08253
ubiquitous expression of MMP-2
Manually annotated by BRENDA team
additional information
-
MMP-2 immunoexpression in all phases of estrous cycle
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
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
-
extracellular matrix
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20000
-
GaCD, without fibronectin-like insert, SDS-PAGE
653757
25920
-
recombinant C domain, elektrospray mass spectrometry
651874
26500
-
recombinant C domain, SDS-PAGE
651874
38000
-
GaCDfn, with fibronectin-like insert, SDS-PAGE
653757
45000
-
active form lacking the C-terminal domain, SDS-PAGE
651872
62000
-
active MMP-2, SDS-PAGE
651301
62000
-
SDS-PAGE
651872
68000
-
proMMP-2, SDS-PAGE
651301
72000
-
-
651863
72000
-
SDS-PAGE
651872
72000
-
-
651874
72000
-
SDS-PAGE
712141
72000
-
pro-MMP-2, SDS-PAGE
712166
72000
-
SDS-PAGE
712625
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 62000, human, active enzyme, SDS-PAGE under reducing conditions
?
-
x * 57000, human, active form, SDS-PAGE
?
-
x * 72000, human, zymogen, SDS-PAGE under reducing conditions
?
-
x * 67000, human, active form, SDS-PAGE under reducing condition
?
-
x * 72000, human, zymogen, SDS-PAGE
?
-
x * 65000, rabbit, latent form, SDS-PAGE under nonreducing conditions, x * 61000, rabbit, active form, SDS-PAGE under nonreducing conditions, x * 72000, rabbit, latent form, SDS-PAGE under reducing conditions
?
-
x * 66000, human, active form, SDS-PAGE
?
-
x * 65000, rabbit, active form, SDS-PAGE under reducing conditions
?
-
x * 66000, SDS-PAGE, x * 66518, calculated, enzyme mutant E404A, x * 59000, SDS-PAGE, x * 47052, calculated, enzyme mutant lacking collagen-binding domain
?
-
x * 72000, proenzyme, x * 62000 and x * 45000, active species, SDS-PAGE
?
-
x * 68000, active MMP-2, SDS-PAGE, x * 72000, proMMP-2, SDS-PAGE
?
-
x * 72000, latent MMP-2, SDS-PAGE, x * 62000, activ MMP-2, SDS-PAGE
?
P08253
x * 72000, native proMMP-2, x * 64000, recombinant MMP-2
?
-
x * 72000, pro-MMP-2, SDS-PAGE, x * 66000, activated MMP-2, SDS-PAGE
?
-
x * 72000, proMMP-2, SDS-PAGE
additional information
-
native and denatured collagen binding properties reside in the fibronectin type II modules of enzyme, that is the collagen binding domain. Enzyme utilizes the collagen binding domain in cis for collagen binding and triple helicase activity
additional information
-
modeling of the interaction of fibrinogen with different truncated forms of MMP-2, i.e. the autoinhibitory procatalytic domain, the catalytic domain, the catalytic domain lacking the fibronectin-like domain, the fibronectin-like domain alone, and the haemopexin-like domain, using crystal structures isolated from the full-length proMMP-2, PDB ID 1CK7, overview
additional information
P08253
proMMP-2 consists of a signal peptide, a pro-peptide, a collagenase-like domain 1, a collagen-binding domain, a collagenase-like domain 2, and a hemopexin-like domain
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
-
activation of 72 kDa proenzyme by aminophenyl-mercuric acetate to 62 and 45 kDa species, no spontaneous autoactivation
phosphoprotein
P08253
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
-
activation
proteolytic modification
-
membrane type MMP-1, MT1-MMP, participates in the activation of gelatinase A, overview
proteolytic modification
-
the proMMP-2 precursor form is cleaved by MT1-MMP to produce an intermediate MMP-2,subsequently, this molecule autocatalytically converts itself into mature MMP-2
additional information
-
activation of pro-MMP-2 by 4-aminophenylmercuric acetate
additional information
-
artificial biotinylation of the purified recombinant CBD domain for library screening, overview
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
LITERATURE
60.8
-
Tm
651048
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
from pulmonary artery smooth muscle plasma membrane
-
as an inactive zymogen, rapid activation by 4-aminophenylmercuric acetate
-
catalytic domain
-
catalytic domain of mutated enzyme
-
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 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
-
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
-
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 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
-
MMP-2 expression analysis in embryonic tissues of wild-type and caireticulin-deficient mice, overview
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
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
-
inhibition of the SDF-1a/CXCR4 axis downregulates the rhOPN-induced MMP-2 expression and activity
-
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
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
E412D
-
site-directed mutagenesis
K50G
-
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
K50R
-
site-directed mutagenesis
additional information
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recombinant collagen binding domain of enzyme, competitive inhibition of gelatin binding to intact enzyme by 73%, inhibition of enzyme-dependent cleavage of an 11 amino acid short protein fragment by less than 10%
additional information
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recombinant enzyme lacking collagen-binding domain, does not block binding to gelatin of either enzyme mutant E404A or matrix metalloproteinase MMP-9 mutant E402A
additional information
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construction of MMP-2 truncation mutants overview, an MMP-2 mutant, with deleted hemopexin-like domain and three fibronectin-like type II domains, and native MMP-2 show similar affinities for APP-IP, chimeric proteases, consisting of various parts of the MMP-2 catalytic domain and those of MMP-7 or MMP-9, show that Ala88 and Gly94 in the non-prime side and Tyr145 and Thr146 in the prime side of the substrate-binding cleft of MMP-2 contribute separately to the selective inhibition bei APP-PI, mutational interaction analysis, overview
Y52A
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site-directed mutagenesis
additional information
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calreticulin-deficient null mice embryos show increased MMP-2 expression and activity, but unaltered TIMP-2 inhibitor levels, the embryos show defects in the heart and body wall, phenotype, overview
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
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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
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
diagnostics
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the MMP-2/TIMP-2 ratio may be of value in evaluating the prognosis in canine oronasal cavity tumors
diagnostics
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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
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attractive therapeutic target for cancer invasion and metastasis, morbidity and mortality of cancer patients are directly related to the ability of tumor cells to metastasize, gelatinase A is required by metastazing tumor cells to traverse basement membrane at tissue bounaries and in blood vessels, therefore this enzyme is a promising target for the development of antitumor drugs
medicine
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inhibitors for use as potential therapeutic agents
medicine
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understanding the detailed molecular structures and the comformational changes of MMP-2 in its zymogen, active, and inhibited states can aid in the rational design of anti-cancer drugs
medicine
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enzyme is the main enzymatic activity of gelatinolysis in oral squamous cell carcinomas. The enzyme form/proform ratio obtained by zymography is significantly higher in T3 and T4 stages than in T1 and T2 stages
medicine
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only a minority of urine samples from patients with bladder cancer show enzyme activity
medicine
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ratio of matrx metalloproteinases MMP-9/MMP-2 is enhanced in cancer patients compared with benign diseases and healthy individuals. No correlation between gelatinolytic activity and high tumoral marker values is found
medicine
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during gastric ulcer healing, enzyme expression as well as matrix metalloproteinase MMP-3 and MMP-13 are induced in stromal cells of the gastric mucosa bordering the ulcer. Gelatinolytic activity is increased during the healing and is associated with extracellular matrix of the healing mucosa and newly formed vessels. Enzyme mRNA is homogenously distributed in all layers of the ulcer bed
medicine
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endogenous urokinase plasminogen activator from cultured hepatic stellate cells significantly induces the active forms of enzyme and matrix metalloproteinase MMP-9 in cirrhotic tissue slices. Transfection of hepatic stellate cells with urokinase plasminogen activator gene results in overactivation of enzyme and matrix metalloproteinases MMP-3 and MMP-9
medicine
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topical treatment of chronic dermal ulcers
additional information
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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