Information on EC 3.4.24.23 - matrilysin and Organism(s) Homo sapiens

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The enzyme appears in selected viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.4.24.23
-
RECOMMENDED NAME
GeneOntology No.
matrilysin
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
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-
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CAS REGISTRY NUMBER
COMMENTARY hide
141256-52-2
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
metabolism
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matrix metalloproteinase-7 is regulated in tuberculosis by a p38 MAPK-dependent, p-aminosalicylic acid-sensitive signaling cascade. The induction is not inhibited by p-aminosalicyclic acid, an agent used to treat drug-resistant tuberculosis. The p38 MAPK pathway regulates the divergence between MMPs and TIMP-1
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-methoxy-coumarin-4-yl)acetyl-Ala-Pro-Lys-2,4-dinitrophenol + H2O
?
show the reaction diagram
-
-
-
-
?
(7-methoxycoumarin-4-yl)-acetyl-L-Pro-L-Leu-Gly-L-Leu-[N3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl]-L-Ala-L-Arg-NH2 + H2O
(7-methoxycoumarin-4-yl)-acetyl-L-Pro-L-Leu-Gly + L-Leu-[N3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl]-L-Ala-L-Arg-NH2
show the reaction diagram
-
-
-
-
?
(7-methoxycoumarin-4-yl)-acetyl-Pro-Leu-Gly-Leu-[N-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl]-Ala-Arg amide + H2O
?
show the reaction diagram
-
-
-
-
?
(7-methoxycoumarin-4-yl)-acetyl-Pro-Leu-Gly-Leu-[N-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl]-L-Ala-L-Arg amide + H2O
?
show the reaction diagram
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-
-
-
?
(7-methoxycoumarin-4-yl)acetyl-L-Pro-L-Leu-Gly-L-Leu-[N3-(2,4-dinitrophenyl)-L-2,3-diamino-propionyl]-L-Ala-L-Arg-NH2 + H2O
?
show the reaction diagram
(7-methoxycoumarin-4-yl)acetyl-L-Pro-L-Leu-Gly-L-Leu-[N3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl]-L-Ala-L-Arg-NH2 + H2O
?
show the reaction diagram
-
MOCAc-PLGL(Dpa)AR
-
?
(7-methoxycoumarin-4-yl)acetyl-L-Pro-Leu-Gly-L-Leu-[N3-2,4-dinitrophenyl-L-2,3-diamino-propionyl]-L-Ala-L-Arg-NH2 + H2O
?
show the reaction diagram
-
MOCAc-PLGL(Dpa)AR
-
?
(7-methoxycoumarin-4-yl)acetyl-LPro-L-Leu-Gly-L-Leu-[N3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl]-L-Ala-L-Arg-NH2 + H2O
?
show the reaction diagram
-
-
-
-
?
(7-methoxycoumarin-4-yl)acetyl-Pro-Leu-Gly-Leu-N-3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl-Ala-Arg-NH2 + H2O
?
show the reaction diagram
-
-
-
-
?
2,4-Dinitrophenyl-Arg-Pro-Leu-Ala-Leu-Trp-Arg-Ser + H2O
?
show the reaction diagram
-
optimized fluorogenic substrate
-
-
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2,4-Dinitrophenyl-Pro-Leu-Gly-Leu-Trp-Ala-D-Arg-NH2 + H2O
2,4-Dinitrophenyl-Pro-Leu-Gly + Leu-Trp-Ala-D-Arg-NH2
show the reaction diagram
7-amino-4-methylcoumaryl-Pro-Lys-Pro-Leu-Ala-Leu-Dap(Dnp)-Ala-Arg-NH2 + H2O
?
show the reaction diagram
-
-
-
-
?
7-methoxycoumarin-4acetylPLGL(L-2,3-diaminopropionyl)AR + H2O
7-methoxycoumarin-4acetyl-PLG + ?
show the reaction diagram
-
-
-
?
7-methoxycoumarin-4acetylPLGL(L-2,3-diaminopropionyl)AR + H2O
?
show the reaction diagram
-
-
-
?
aggrecan + H2O
?
show the reaction diagram
-
-
-
?
alpha1PI + H2O
?
show the reaction diagram
-
protein, inhibitor of elastase, inactivation by cleavage of Pro357-Met358 peptide bond of its reactive centre
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-
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annexin II + H2O
?
show the reaction diagram
-
treatment of human colon cancer cell lines with active matrilysin releases a 35 kDa annexin II form, which lacked its N-terminal region, into the culture supernatant. The release of the 35 kDa annexin II by matrilysin is significantly enhanced in the presence of serotonin or heparin. Matrilysin hydrolyzes annexin II at the Lys9-Leu10 bond, thus dividing the protein into an N-terminal nonapeptide and the C-terminal 35 kDa fragment. The nonapeptide generated by matrilysin treatment might be anchored to the cell membrane, possibly by binding to intact annexin II, and interact with tissue-type plasminogen activator via its C-terminal lysine
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-
?
Azocoll + H2O
?
show the reaction diagram
beta-casein + H2O
?
show the reaction diagram
C-type lectin domain family 3 member A + H2O
?
show the reaction diagram
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i.e. CLEC3A. MMP-7 cleaves the 20 kDa CLEC3A protein, dividing it to a 15 kDa COOH-terminal fragment and an NH2-terminal fragment with the basic sequence. The 15 kDa fragment no longer has heparin-binding activity. Treatment of the CLEC3A-expressing cells with MMP-7 releases the 15 kDa CLEC3A into the culture supernatant. The native 20 kDa CLEC3A promotes cell adhesion to laminin-332 and fibronectin substrates, but this activity is abrogated by the cleavage by MMP-7
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-
?
cartilage + H2O
?
show the reaction diagram
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-
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?
casein + H2O
?
show the reaction diagram
Collagen + H2O
?
show the reaction diagram
-
-
-
-
?
collagen type IV + H2O
?
show the reaction diagram
-
-
-
?
Cy5.5-M7 peptide + H2O
?
show the reaction diagram
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method development for in vivo detection and quantitation of MMP7 activity, in tumors induces in nude mice by injection of human SW480 colon cancer cells, using a specific near-infrared polymer-based proteolytic beacon, PB-M7NIR. PB-M7NIR is a pegylated polyamidoamine PAMAM-Generation 4 dendrimer core covalently coupled to a Cy5.5 labeled peptide representing a selective substrate that monitors MMP7 activity and AF750 as an internal reference to monitor relative substrate concentration. In vivo imaging of tumors expressing MMP7 has a median S/R ratio 2.2-fold higher than a bilateral control tumor, quantitative detection method with ability of substrate PB-M7NIR to effectively localize and assess MMP7 activity in the tumor microenvironment, development and evaluation, overview
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dansyl-PLALWAR + H2O
?
show the reaction diagram
-
synthetic fluorescent peptide
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?
decorin + H2O
transforming growth factor-beta + ?
show the reaction diagram
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-
-
?
E-cadherin + H2O
modified E-cadherin + E-cadherin ectodomain
show the reaction diagram
-
matrilysin cleaves E-cadherin in its juxtamembrane stalk releasing the entire ectodomain
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?
Elastin + H2O
?
show the reaction diagram
elastin + H2O
elastin peptides
show the reaction diagram
FasL + H2O
sFasL + ?
show the reaction diagram
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human and murine FasL
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?
fibrin + H2O
fibrin fragments + ?
show the reaction diagram
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-
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?
fibronactin + H2O
fibronectin peptide fragments
show the reaction diagram
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MWs of 30 to 175 kDa
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?
fibronecin + H2O
?
show the reaction diagram
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pericellular proteolysis
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?
Fibronectin + H2O
?
show the reaction diagram
Gelatin + H2O
?
show the reaction diagram
Gly-Pro-Gln-Ala-Ile-Ala-Gly-Gln + H2O
?
show the reaction diagram
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Gly-Pro-Gln-Gly-Ile-Ala-Gly-Gln + H2O
?
show the reaction diagram
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-
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Gly-Pro-Gln-Gly-Ile-Ala-Met-Gln + H2O
?
show the reaction diagram
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Gly-Pro-Gln-Gly-Leu-Ala-Gly-Gln + H2O
?
show the reaction diagram
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-
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Gly-Pro-Met-Gly-Ile-Ala-Gly-Gln + H2O
?
show the reaction diagram
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IGFBP-3 + H2O
?
show the reaction diagram
insulin-like growth factor binding protein-2 + H2O
?
show the reaction diagram
insulin-like growth factor binding protein-5 + H2O
?
show the reaction diagram
kappa-casein + H2O
?
show the reaction diagram
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-
-
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?
Laminin + H2O
?
show the reaction diagram
Laminin-1 + H2O
?
show the reaction diagram
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laminin-332 + H2O
?
show the reaction diagram
laminin-5/Laminin-322 + H2O
90 kDa beta3 chain fragment + ?
show the reaction diagram
-
i.e. LN5, composed of alpha3, beta3,and gamma2 chains, is an important component of epithelial basement membranes where it induces firm adhesion and hemidesmosome formation, LN5 and MMP7 are coexpressed in HT29 cells, as well as in HT29 xenograft tumors and human colorectal adenocarcinomas, MMP7-processed LN5 significantly enhances cell motility, overview
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?
laminin-5/laminin-332 + H2O
90 kDa beta3 chain fragment + ?
show the reaction diagram
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i.e. LN5, specific proteolysis by MMP7 in the beta3 chain at Ala515-Ile516, overview
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?
N-cadherin + H2O
?
show the reaction diagram
osteopontin + H2O
?
show the reaction diagram
-
-
-
?
Oxidized alpha1PI + H2O
?
show the reaction diagram
-
cleavage of Phe352-Leu353 bond
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perlecan + H2O
?
show the reaction diagram
pro-alpha-defensin + H2O
alpha-defensin + alpha-defensin propeptide
show the reaction diagram
-
-
-
-
?
pro-alpha-defensin-1 + H2O
alpha-defensin-1 + alpha-defensin-1 propeptide
show the reaction diagram
-
i.e. procryptdins
-
-
?
pro-beta-defensin + H2O
beta-defensin + beta-defensin propeptide
show the reaction diagram
-
-
-
-
?
pro-HNP-1 + H2O
HNP-1 + HNP-1 propeptide
show the reaction diagram
Pro-matrix metalloproteinase 1 + H2O
?
show the reaction diagram
-
activation by specific cleavage at the Gln80-Phe81 bond
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-
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proADAM28s + H2O
ADAM28s + propeptide
show the reaction diagram
-
secreted form of a member of a disintegrin and metalloproteinase family. ProADAM28s is processed by enzyme to active 42 and 40 kDa forms lacking the propeptide
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?
Proteoglycan + H2O
?
show the reaction diagram
syndecan-2 + H2O
?
show the reaction diagram
tumor-associated antigen 90K + H2O
?
show the reaction diagram
type IV basement membrane collagen + H2O
?
show the reaction diagram
-
-
-
?
Type IV collagen + H2O
?
show the reaction diagram
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
beta-casein + H2O
?
show the reaction diagram
-
-
-
-
?
Collagen + H2O
?
show the reaction diagram
-
-
-
-
?
E-cadherin + H2O
modified E-cadherin + E-cadherin ectodomain
show the reaction diagram
-
matrilysin cleaves E-cadherin in its juxtamembrane stalk releasing the entire ectodomain
-
-
?
elastin + H2O
elastin peptides
show the reaction diagram
-
degradation
in the range of 500-8000 Da
-
?
fibronactin + H2O
fibronectin peptide fragments
show the reaction diagram
-
-
MWs of 30 to 175 kDa
-
?
Fibronectin + H2O
?
show the reaction diagram
-
also MMP-7-catalyzed cleavages of chymotryptic fragments of fibronectin by cell-bound MMP-7, overview
-
-
?
IGFBP-3 + H2O
?
show the reaction diagram
-
i.e. insulin-like growth factor binding protein 3, proteolysis by enzyme plays a crucial role in regulating IGF-I bioavailability, thereby promoting cell survival
-
-
?
insulin-like growth factor binding protein-2 + H2O
?
show the reaction diagram
-
MMP-7 generates IGF-IIand triggers its matricine action by degradation of the IGF-II/IGFBP-2 complex binding to heparan sulfate proteoglycan in the extracellular matrix, MMP-7 induces phosphorylation of the insulin-like growth factor type-1 receptor in colon cancer cells involving IGF-II but not IGFBP-2, overview
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?
insulin-like growth factor binding protein-5 + H2O
?
show the reaction diagram
-
in the medium of gastric myofibroblasts, knockdown of IGFBP-5 abolished the myofibroblast proliferation response to MMP-7, overview
-
-
?
laminin-332 + H2O
?
show the reaction diagram
-
pericellular substrate
-
-
?
laminin-5/Laminin-322 + H2O
90 kDa beta3 chain fragment + ?
show the reaction diagram
-
i.e. LN5, composed of alpha3, beta3,and gamma2 chains, is an important component of epithelial basement membranes where it induces firm adhesion and hemidesmosome formation, LN5 and MMP7 are coexpressed in HT29 cells, as well as in HT29 xenograft tumors and human colorectal adenocarcinomas, MMP7-processed LN5 significantly enhances cell motility, overview
-
-
?
N-cadherin + H2O
?
show the reaction diagram
-
recombinant active MMP-7 increases the amount of N-cadherin fragment by 82% and augments apoptosis by 53%
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-
?
perlecan + H2O
?
show the reaction diagram
-
i.e. HSPG2, a large heparan sulfate proteoglycan, expressed in the basement membrane underlying epithelial and endothelial cells, proteolytic degradation
-
-
?
pro-alpha-defensin + H2O
alpha-defensin + alpha-defensin propeptide
show the reaction diagram
-
-
-
-
?
pro-alpha-defensin-1 + H2O
alpha-defensin-1 + alpha-defensin-1 propeptide
show the reaction diagram
-
i.e. procryptdins
-
-
?
pro-beta-defensin + H2O
beta-defensin + beta-defensin propeptide
show the reaction diagram
-
-
-
-
?
pro-HNP-1 + H2O
HNP-1 + HNP-1 propeptide
show the reaction diagram
-
i.e. pro-human neutrophil peptide-1, in a cell-based assay system
-
-
?
syndecan-2 + H2O
?
show the reaction diagram
-
MMP-7 cleaves the N-terminal Leu149 residue in the extracellular domain of syndecan-2 to a product of about 45 kDa, MALDI-TOF MS analysis, overview
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?
tumor-associated antigen 90K + H2O
?
show the reaction diagram
-
-
-
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?
Type IV collagen + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
NaCl
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wild-type and Y219F mutant MMP-7 activity is enhanced with increasing concentration of NaCl, activation by 550% and 850% at 4 M NaCl, respectively
additional information
-
metalloprotease
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(-)-5-hydroxypluviatolide
-
50% inhibition at 0.05 mM
(-)-catechin-3-gallate
(-)-epicatechin-3-gallate
(-)-epigallo-3-catechin gallate
-
-
(-)-epigallocatechin-3-gallate
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inhibitory effect is increased on presence of 10 mM CaCl2, no interaction with Cl-
(-)-gallocatechin-3-gallate
(-)-haplomyrfolin
-
50% inhibition at 0.1 mM
(-)-hinokinin
-
50% inhibition at 0.1 mM
(-)-thujaplicatin-d3
-
50% inhibition at 0.08 mM
(4-phenyl-1,4-dihydropyridine-3,5-diyl)dimethanol
-
-
1,10-phenanthroline
-
-
1-(4-methoxyphenyl)sulfonyl-4-(tert-butoxycarbonyl)-piperazine-2-carboxylic acid
-
-
1-butanol
-
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2-butanol
-
-
2-methyl-1-propanol
-
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2-methyl-2-butanol
-
-
2-Methyl-2-propanol
-
-
3,9-di(4-methoxylphenyl)-6,12-diphenyl-3,9-diazahexacyclo[6.4.0.02,7.04,11.05,10]dodecane-1,5,7,11-tetracarboxylate
-
-
3,9-di(4-methylphenyl)-6,12-diphenyl-3,9-diazahexacyclo[6.4.0.02,7.04,11.05,10]dodecane-1,5,7,11-tetracarboxylate
-
-
3,9-dibenzyl-1,5,7,11-tetrahydroxymethyl-6,12-di(2,3,4-trimethoxylphenyl)-3,9-diazahexacyclo[6.4.0.02,7.04,11.05,10]dodecane
-
-
3,9-dibenzyl-1,5,7,11-tetrahydroxymethyl-6,12-di(2,4,5-trimethoxylphenyl)-3,9-diazahexacyclo[6.4.0.02,7.04,11.05,10]dodecane
-
-
3,9-dibenzyl-1,5,7,11-tetrahydroxymethyl-6,12-di(2,4-dimethoxylphenyl)-3,9-diazahexacyclo[6.4.0.02,7.04,11.05,10]dodecane
-
-
3,9-dibenzyl-1,5,7,11-tetrahydroxymethyl-6,12-di(4-hydroxyphenyl)-3,9-diazahexacyclo[6.4.0.02,7.04,11.05,10]dodecane
-
-
3,9-dibenzyl-6,12-di(2,3,4-trimethoxylphenyl)-3,9-diazahexacyclo[6.4.0.02,7.04,11.05,10]dodecane-1,5,7,11-tetracarboxylate
-
-
3,9-dibenzyl-6,12-di(2,4,5-trimethoxylphenyl)-3,9-diazahexacyclo[6.4.0.02,7.04,11.05,10]dodecane-1,5,7,11-tetracarboxylate
-
-
3,9-dibenzyl-6,12-di(2,4-dimethoxylphenyl)-3,9-diazahexacyclo[6.4.0.02,7.04,11.05,10]dodecane-1,5,7,11-tetracarboxylate
-
-
3,9-dibenzyl-6,12-di(3,4,5-trimethoxylphenyl)-3,9-diazahexacyclo[6.4.0.02,7.04,11.05,10]dodecane-1,5,7,11-tetracarboxylate
-
-
3,9-dibenzyl-6,12-di(4-hydroxyphenyl)-3,9-diazahexacyclo[6.4.0.02,7.04,11.05,10]dodecane-1,5,7,11-tetracarboxylate
-
-
3,9-dibenzyl-6,12-di(4-methoxylphenyl)-3,9-diazahexacyclo[6.4.0.02,7.04,11.05,10]dodecane-1,5,7,11-tetracarboxylate
-
-
3,9-dibenzyl-6,12-diphenyl-3,9-diazahexacyclo[6.4.0.02,7.04,11.05,10]dodecane-1,5,7,11-tetracarboxylate
-
-
3,9-diphenyl-6,12-di(4-fluoridephenyl)-3,9-diazahexacyclo[6.4.0.02,7.04,11.05,10]dodecane-1,5,7,11-tetracarboxylate
-
-
3,9-diphenyl-6,12-di(4-hydroxyphenyl)-3,9-diazahexacyclo[6.4.0.02,7.04,11.05,10]dodecane-1,5,7,11-tetracarboxylate
-
-
3,9-diphenyl-6,12-di(4-methoxylphenyl)-3,9-diazahexacyclo[6.4.0.02,7.04,11.05,10]dodecane-1,5,7,11-tetracarboxylate
-
-
3,9-diphenyl-6,12-di(4-methylphenyl)-3,9-diazahexacyclo[6.4.0.02,7.04,11.05,10]dodecane-1,5,7,11-tetracarboxylate
-
-
3,9-diphenyl-6,12-diphenyl-3,9-diazahexacyclo[6.4.0.02,7.04,11.05,10]dodecane-1,5,7,11-tetracarboxylate
-
-
3.9-diphenyl-6,12-di(3,4,5-trimethoxylphenyl)-3,9-diazahexacyclo[6.4.0.02,7.04,11.05,10]dodecane-1,5,7,11-tetracarboxylate
-
-
6,12-di(2,3,4-trimethoxylphenyl)-3,9-diazahexacyclo[6.4.0.02,7.04,11.05,10]dodecane-1,5,7,11-tetracarboxylate
-
-
6,12-di(2,4,5-trimethoxylphenyl)-3,9-diazahexacyclo[6.4.0.02,7.04,11.05,10]dodecane-1,5,7,11-tetracarboxylate
-
-
6,12-di(2,4-dimethoxylphenyl)-3,9-diazahexacyclo[6.4.0.02,7.04,11.05,10]dodecane-1,5,7,11-tetracarboxylate
-
-
6,12-di(3,4,5-trimethoxylphenyl)-3,9-diazahexacyclo[6.4.0.02,7.04,11.05,10]dodecane-1,5,7,11-tetracarboxylate
-
-
6,12-di(4-hydroxyphenyl)-3,9-diazahexacyclo[6.4.0.02,7.04,11.05,10]dodecane-1,5,7,11-tetracarboxylate
-
-
6,12-di(4-methoxylphenyl)-3,9-diazahexacyclo[6.4.0.02,7.04,11.05,10]dodecane-1,5,7,11-tetracarboxylate
-
-
6,12-diphenyl-3,9-diazahexacyclo[6.4.0.02,7.04,11.05,10]dodecane-1,5,7,11-tetracarboxylate
-
-
Ag-3340
-
-
andrographolide
-
a diterpenoid lactone isolated from a traditional herbal medicine Andrographis paniculata, downregulates MMP-7 in colorectal carcinoma LoVo cells leading to inhibition of cell migration and invasion, overview
batimastat
-
i.e. BB-94, BB-94 significantly reduces the amount of N-cadherin fragment produced in response to Fas-L
Brij-35
-
activates MMP-7 in a broad concentration range, but inhibits at high concentration
cardiolipin
-
associates with the enzyme at the cell surface and inhibits by 92%
Cholesterol sulfate
diethyl 1-phenoxy-4-(4-propylphenyl)-1,4-dihydropyridine-3,5-dicarboxylate
-
-
diethyl 4-(2-methoxyphenyl)-1,4-dihydropyridine-3,5-dicarboxylate
-
-
diethyl 4-(2-nitrophenyl)-1,4-dihydropyridine-3,5-dicarboxylate
-
-
diethyl 4-(3-methoxyphenyl)-1,4-dihydropyridine-3,5-dicarboxylate
-
-
diethyl 4-(3-nitrophenyl)-1,4-dihydropyridine-3,5-dicarboxylate
-
-
diethyl 4-(4-methylphenyl)-1,4-dihydropyridine-3,5-dicarboxylate
-
-
diethyl 4-(4-nitrophenyl)-1,4-dihydropyridine-3,5-dicarboxylate
-
-
diethyl 4-(4-nitrophenyl)-1-phenoxy-1,4-dihydropyridine-3,5-dicarboxylate
-
-
diethyl 4-(4-propylphenyl)-1,4-dihydropyridine-3,5-dicarboxylate
-
-
diethyl 4-[4-(5-methoxypentyl)phenyl]-1,4-dihydropyridine-3,5-dicarboxylate
-
-
diethyl 4-[4-(5-methoxypentyl)phenyl]-1-phenoxy-1,4-dihydropyridine-3,5-dicarboxylate
-
-
dimethyl sulfoxide
-
competitive inhibition
fibronectin 1
-
fibronectin 1, interacts with MMP-7
-
GM6001
green tea catechin
-
-
-
Hydroxamate
-
-
KB-R7785
-
-
marimastat
-
-
methyl 1-(4-methoxyphenyl)sulfonyl-4-(N-methyl-N-hexylaminocarbonyl)piperazine-2-carboxylate
-
-
methyl 1-(4-methoxyphenyl)sulfonyl-4-(tert-butoxycarbonyl)piperazine-2-carboxylate
-
-
methyl 1-(4-methoxyphenyl)sulfonyl-4-acetylpiperazine-2-carboxylate
-
-
methyl 1-(4-methoxyphenyl)sulfonyl-4-amidopiperazine-2-carboxylate
-
-
methyl 1-(4-methoxyphenyl)sulfonyl-4-cyclohexanecarbonylpiperazine-2-carboxylate
-
-
methyl 1-(4-methoxyphenyl)sulfonyl-4-methylpiperazine-2-carboxylate
-
-
methyl 1-(4-methoxyphenyl)sulfonyl-4-methylsulfonylpiperazine-2-carboxylate
-
-
methyl 1-(4-methoxyphenyl)sulfonylpiperazine-2-carboxylate hydrochloride
-
-
methyl 4-[4-(4-bromophenyl)thiazol-2-yl]-1-(4-methoxyphenyl)sulfonylpiperazine-2-carboxylate
-
-
MMPI-II
-
a small synthetic inhibitor of 514 Da
N-(R)-(2-(hydroxyaminocarbonyl)methyl)-4-methylpentanoyl-L-naphthyalanyl-L-alanine-2-aminoethyl amide
-
i.e. TAPI-1, a hydroxamate-based metalloproteinase inhibitor
-
N-alkylpiperazine
-
-
N-hydroxy-1,4-bis(4-methoxyphenylsulfonyl)piperazine-2-carboxamide
-
-
N-hydroxy-1-(4-bromophenyl)sulfonyl-4-(N-methyl-N-hexylaminocarbonyl)piperazine-2-carboxamide
-
-
N-hydroxy-1-(4-bromophenyl)sulfonyl-4-(S)-(2-hydroxy-3-methyl-1-oxobutyl)piperazine-2-carboxamide
-
-
N-hydroxy-1-(4-bromophenyl)sulfonyl-4-[N-bis(2-methoxyethyl)aminocarbonyl]piperazine-2-carboxamide
-
-
N-hydroxy-1-(4-methoxyphenyl)sulfonyl-4-(1-oxohexyl)piperazine-2-carboxamide
-
-
N-hydroxy-1-(4-methoxyphenyl)sulfonyl-4-(2-phenylethylaminocarbonyl)piperazine-2-carboxamide
-
-
N-hydroxy-1-(4-methoxyphenyl)sulfonyl-4-(3-ethoxy-1-propoxycarbonyl)piperazine-2-carboxamide
-
-
N-hydroxy-1-(4-methoxyphenyl)sulfonyl-4-(3-methoxyphenylaminocarbonyl)piperazine-2-carboxamide
-
-
N-hydroxy-1-(4-methoxyphenyl)sulfonyl-4-(3-pyridinylmethoxycarbonyl)piperazine-2-carboxamide
-
-
N-hydroxy-1-(4-methoxyphenyl)sulfonyl-4-(4-biphenylcarbonyl)piperazine-2-carboxamide
-
-
N-hydroxy-1-(4-methoxyphenyl)sulfonyl-4-(4-methyl-1,2,3-thiadiazole-5-carbonyl)piperazine-2-carboxamide
-
-
N-hydroxy-1-(4-methoxyphenyl)sulfonyl-4-(4-morpholinylcarbonyl)piperazine-2-carboxamide
-
-
N-hydroxy-1-(4-methoxyphenyl)sulfonyl-4-(5-methyl-3-phenylisoxazole-4-carbonyl)piperazine-2-carboxamide
-
-
N-hydroxy-1-(4-methoxyphenyl)sulfonyl-4-(isoxazole-5-carbonyl)piperazine-2-carboxamide
-
-
N-hydroxy-1-(4-methoxyphenyl)sulfonyl-4-(n-hexyl)piperazine-2-carboxamide
-
-
N-hydroxy-1-(4-methoxyphenyl)sulfonyl-4-(n-hexylaminocarbonyl)piperazine-2-carboxamide
-
-
N-hydroxy-1-(4-methoxyphenyl)sulfonyl-4-(N-methyl-N-hexylaminocarbonyl)piperazine-2-carboxamide
-
-
N-hydroxy-1-(4-methoxyphenyl)sulfonyl-4-(N-methyl-N-phenylmethylaminocarbonyl)piperazine-2-carboxamide
-
-
N-hydroxy-1-(4-methoxyphenyl)sulfonyl-4-(N-methylpiperazine-1N-carbonyl)piperazine-2-carboxamide hydrochloride
-
-
N-hydroxy-1-(4-methoxyphenyl)sulfonyl-4-(N-propyl-N-cyclopropylmethyl aminocarbonyl)piperazine-2-carboxamide
-
-
N-hydroxy-1-(4-methoxyphenyl)sulfonyl-4-(tert-butoxycarbonyl)piperazine-2-carboxamide
-
-
N-hydroxy-1-(4-methoxyphenyl)sulfonyl-4-acetylpiperazine-2-carboxamide
-
-
N-hydroxy-1-(4-methoxyphenyl)sulfonyl-4-amidopiperazine-2-carboxamide
-
-
N-hydroxy-1-(4-methoxyphenyl)sulfonyl-4-benzoylpiperazine-2-carboxamide
-
-
N-hydroxy-1-(4-methoxyphenyl)sulfonyl-4-benzylcarbamoylpiperazine-2-carboxamide
-
-
N-hydroxy-1-(4-methoxyphenyl)sulfonyl-4-benzyloxycarbonylpiperazine-2-carboxamide
-
-
N-hydroxy-1-(4-methoxyphenyl)sulfonyl-4-benzylthiocarbamoylpiperazine-2-carboxamide
-
-
N-hydroxy-1-(4-methoxyphenyl)sulfonyl-4-cyclohexanecarbonylpiperazine-2-carboxamide
-
-
N-hydroxy-1-(4-methoxyphenyl)sulfonyl-4-furoylpiperazine-2-carboxamide
-
-
N-hydroxy-1-(4-methoxyphenyl)sulfonyl-4-methylpiperazine-2-carboxamide
-
-
N-hydroxy-1-(4-methoxyphenyl)sulfonyl-4-nicotinoylpiperazine-2-carboxamide hydrochloride
-
-
N-hydroxy-1-(4-methoxyphenyl)sulfonyl-4-phenoxyacetylpiperazine-2-carboxamide
-
-
N-hydroxy-1-(4-methoxyphenyl)sulfonyl-4-phenylmethylpiperazine-2-carboxamide
-
-
N-hydroxy-1-(4-methoxyphenyl)sulfonyl-4-thiophenecarbonylpiperazine-2-carboxamide
-
-
N-hydroxy-1-(4-methoxyphenyl)sulfonyl-4-[(3,5-dimethyl-4-isoxazolyl)sulfonyl]piperazine-2-carboxamide
-
-
N-hydroxy-1-(4-methoxyphenyl)sulfonyl-4-[(hexahydro-1H-azepin-1-yl)carbonyl]piperazine-2-carboxamide
-
-
N-hydroxy-1-(4-methoxyphenyl)sulfonyl-4-[2-amino-4-methyl-5-thiazolylsulfonyl]piperazine-2-carboxamide
-
-
N-hydroxy-1-(4-methoxyphenyl)sulfonylpiperazine-2-carboxamide
-
-
N-hydroxy-4-[4-(4-bromophenyl)thiazol-2-yl]-1-(4-methoxyphenyl)sulfonylpiperazine-2-carboxamide
-
-
N-[3-[3,5-bis(hydroxymethyl)-1,4-dihydropyridin-4-yl]phenyl]acetamide
-
-
N-[3-[3,5-bis(hydroxymethyl)-1-phenoxy-1,4-dihydropyridin-4-yl]phenyl]acetamide
-
-
o-phenanthroline
-
-
R-94138
-
-
RRS269
-
-
Sulfatide
-
associates with the enzyme at the cell surface and inhibits by 80%
Sulfodiimine
-
-
TAPI-1
-
a hydroxamate-based matrix metalloproteinase inhibitor, reduces the affinity of the enzyme for cholesterol sulfate and cardiolipin, but not for sulfatide, molecular mechanism by which TAPI-1 inhibits binding of MMP-7 to the lipids, overview
thiorphan
-
-
TIMP-1
-
TIMP-2
-
-
-
TIMP-3
-
TIMP-4
-
tissue inhibitor of metalloproteinases-4
-
TIMP3
-
tissue inhibitor of metalloproteinase-3, interacts with MMP-7
-
Tissue inhibitor of metalloproteinase-1
-
-
-
tissue inhibitors of metalloproteinase 1
-
TIMP-1
-
Zincov
-
-
ZnCl2
-
-
[4-(2,4-dimethoxyphenyl)-1-phenoxy-1,4-dihydropyridine-3,5-diyl]dimethanol
-
-
[4-(3,4,5-trimethoxyphenyl)-1,4-dihydropyridine-3,5-diyl]dimethanol
-
-
[4-(4-methoxyphenyl)-1,4-dihydropyridine-3,5-diyl]dimethanol
-
-
[4-(4-nitrophenyl)-1,4-dihydropyridine-3,5-diyl]dimethanol
-
-
[4-(4-propylphenyl)-1,4-dihydropyridine-3,5-diyl]dimethanol
-
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Brij-35
-
activates MMP-7 in a broad concentration range, but inhibits at high concentration
Cholesterol sulfate
-
selectively alters substrate preference of matrix metalloproteinase-7 and promotes degradations of pericellular laminin-332 and fibronectin. Degradation of laminin-332 (laminin-5) catalyzed by MMP-7 is accelerated dramatically in the presence of cholesterol sulfate, whereas the sulfated lipid inhibits the degradation of casein catalyzed by the protease. Cholesterol sulfate facilitates the proteolyses by cross-linking MMP-7 to its substrates, mechanism, overview
Fas ligand
-
treatment with Fas ligand, Fas-L, increases levels of active MMP-7 by 80%
-
heparin
-
porcine intestinal heparin, increases activity by decreasing the Km value, increases the enzyme's thermostability
plasmin
-
-
-
syndecan-2
-
enhances both expression and secretion of MMP-7, directly interacts with pro-MMP-7, and potentiates the enzymatic activity of pro-MMP-7 by activating its processing into the active MMP-7. Syndecan-2 functions as a docking receptor for pro-MMP-7 in colon cancer cells, overview
-
Trypsin
-
-
-
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.019 - 0.057
(7-methoxycoumarin-4-yl)-acetyl-L-Pro-L-Leu-Gly-L-Leu-[N3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl]-L-Ala-L-Arg-NH2
0.028
(7-methoxycoumarin-4-yl)acetyl-L-Pro-Leu-Gly-L-Leu-[N3-2,4-dinitrophenyl-L-2,3-diamino-propionyl]-L-Ala-L-Arg-NH2
-
pH 7.5, 25C
0.0511 - 0.211
(7-methoxycoumarin-4-yl)acetyl-LPro-L-Leu-Gly-L-Leu-[N3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl]-L-Ala-L-Arg-NH2
0.026
2,4-Dinitrophenyl-Arg-Pro-Leu-Ala-Leu-Trp-Arg-Ser
-
-
0.065
2,4-dinitrophenyl-Pro-Leu-Gly-Leu-Trp-Ala-D-Arg
-
-
0.0079 - 0.024
dansyl-PLALWAR
0.81
Gly-Pro-Gln-Ala-Ile-Ala-Gly-Gln
-
-
2
Gly-Pro-Gln-Gly-Ile-Ala-Gly-Gln
-
-
2.3
Gly-Pro-Gln-Gly-Ile-Ala-Met-Gln
-
-
7.3
Gly-Pro-Gln-Gly-Leu-Ala-Gly-Gln
-
-
4.2
Gly-Pro-Met-Gly-Ile-Ala-Gly-Gln
-
-
additional information
additional information
-
Km-value decreases from 2.57 mg/ml to 2.29 mg/ml upon nitration of 4-5 Tyr residues of enzyme, pH 7.5, 25C
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.61 - 6.43
(7-methoxycoumarin-4-yl)acetyl-LPro-L-Leu-Gly-L-Leu-[N3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl]-L-Ala-L-Arg-NH2
5
2,4-Dinitrophenyl-Arg-Pro-Leu-Ala-Leu-Trp-Arg-Ser
-
-
3.5
2,4-dinitrophenyl-Pro-Leu-Gly-Leu-Trp-Ala-D-Arg
-
-
0.00051 - 6.08
dansyl-PLALWAR
0.472
Gly-Pro-Gln-Ala-Ile-Ala-Gly-Gln
-
-
0.222
Gly-Pro-Gln-Gly-Ile-Ala-Gly-Gln
-
-
1.17
Gly-Pro-Gln-Gly-Ile-Ala-Met-Gln
-
-
2.47
Gly-Pro-Gln-Gly-Leu-Ala-Gly-Gln
-
-
1.92
Gly-Pro-Met-Gly-Ile-Ala-Gly-Gln
-
-
additional information
additional information
-
kcat-value decreases from 337 mg/ml x M x s to 305 mg/ml x M x s upon nitration of 4-5 Tyr residues of enzyme, pH 7.5, 25C
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
26 - 87
(7-methoxycoumarin-4-yl)acetyl-LPro-L-Leu-Gly-L-Leu-[N3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl]-L-Ala-L-Arg-NH2
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00144
(-)-catechin-3-gallate
-
pH 7.5, 25C
0.00047
(-)-epicatechin-3-gallate
-
pH 7.5, 25C
0.00165
(-)-epigallo-3-catechin gallate
-
pH 7.5, 25C
0.00106
(-)-gallocatechin-3-gallate
-
pH 7.5, 25C
670
1-butanol
-
pH 7.5, 25C
11700
2-butanol
-
pH 7.5, 25C
660
2-methyl-1-propanol
-
pH 7.5, 25C
780
2-methyl-2-butanol
-
pH 7.5, 25C
820
2-Methyl-2-propanol
-
pH 7.5, 25C
0.011
Cholesterol sulfate
-
pH 7.5, 25C
590
dimethyl sulfoxide
-
pH 7.5, 25C
0.000027 - 0.000053
MMPI-II
0.0105
R-94138
-
pH 7.5, 25C
0.0112 - 0.015
thiorphan
0.000009 - 0.000064
TIMP-2
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00001
batimastat
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
4.6
Brij-35
Homo sapiens
-
pH 7.5, 25C
0.0006
cardiolipin
Homo sapiens
-
pH 8.0, 25C
0.0007
Sulfatide
Homo sapiens
-
pH not specified in the publication, 37C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5
-
2,4-dinitrophenyl-Pro-Leu-Gly-Leu-Trp-Ala-D-Arg
7 - 8.5
-
assay at
7.5 - 8
-
assay at
additional information
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 10
-
-
4.5 - 8.5
-
4.5: about 40% of activity maximum, 8.5: about 65% of activity maximum, 2,4-dinitrophenyl-Pro-Leu-Gly-Leu-Trp-Ala-D-Arg
4.5 - 9.5
-
-
5 - 9
-
maximal activity range of wild-type enzyme, and mutants Y193F and Y216F
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25 - 37
-
assay at
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 37
-
-
37 - 55
-
-
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
high MMP-7 expression level
Manually annotated by BRENDA team
-
immunohistochemical expression analysis of MMP-7 in the tumor epithelium and stroma, overview
Manually annotated by BRENDA team
-
immunohistochemical expression analysis of MMP-7 in the tumor epithelium and stroma, overview
Manually annotated by BRENDA team
-
MMP-7 activity is higher in amnion from premature rupture of membranes compared to cesarean delivery, overview
Manually annotated by BRENDA team
-
immunohistochemic detection of MMP7 expression in biliary tract cancer, semi-quantitative RT-PCR and real-time RT-PCR, overview
Manually annotated by BRENDA team
-
from umbilical cord, MMP-7 quantification, overview
Manually annotated by BRENDA team
-
the matrix metalloproteinases MMP-2, MMP-3, MMP-7, MMP-9, and MMP-13 are highly expressed in the tumor-bone microenvironment, and, of these, MMP-7 and MMP-9 are found to be localized to bone-resorbing osteoclasts in human breast-to-bone metastases
Manually annotated by BRENDA team
-
primary tumors
Manually annotated by BRENDA team
-
early stage primary cancers, MMP-7 correlates with breast cancer development, overexpression of MMP-7 and ErbB4, overview
Manually annotated by BRENDA team
-
induction of enzyme expression by TNF-alpha and interleukin IL-1beta
Manually annotated by BRENDA team
-
rectal carcinoma cell
Manually annotated by BRENDA team
MMP7 is secreted mainly by tumor cells instead of matrix cells in colorectal cancer
Manually annotated by BRENDA team
-
expression of matrix metalloproteinases MMP-1, MMP-7 and MMP-10 by migrating enterocytes bordering intestinal ulcers
Manually annotated by BRENDA team
-
low expression of MMP-7, which is induced by physiological processes such as wound healing, but also malignant transformation of epidermal cells
Manually annotated by BRENDA team
-
i.e. ELF, proMMP-7 protein is not detectable in any of the 3 HIV1- groups, including HIV1- smokers with early emphysema. In contrast, ELF pro-MMP-7 is readily detectable in the ELF of HIV1+ smokers with early emphysema
Manually annotated by BRENDA team
-
expression and activity of MMP-7 in fetal membranes during premature rupture of membranes, immunohistochemic analysis, overview
Manually annotated by BRENDA team
-
connective tissue
Manually annotated by BRENDA team
-
highly variable MMP-7 expression in the glioma population
Manually annotated by BRENDA team
-
endometrial carcinoma-derived cell line
Manually annotated by BRENDA team
-
higher expression in epithelium compared to stroma, expression in proximal and distal convoluted tubules and collecting duct, and weakly in renal corpuscles and mesangial cells, podocytes, and Bowman's capsule of glomerules, overview
Manually annotated by BRENDA team
-
infiltrating
Manually annotated by BRENDA team
-
primary, monocyte-derived
Manually annotated by BRENDA team
-
primary cutaneous and metastatic melanoma
Manually annotated by BRENDA team
-
frp, peripheral blood
Manually annotated by BRENDA team
-
primary
Manually annotated by BRENDA team
-
MMP-7 expression analysis of 106 different samples, higher enzyme levels in squamous compared to adenocarcinomas, MMP-7 expression increases the cell proliferation and is correlated to Wnt1 expression,overview
Manually annotated by BRENDA team
-
strong expression of MMP-7 in epithelial dysplasia with a two-phase appearance: a clear demarcation of MMP-7-immunopositive (+) lower dysplastic/basaloid cells from non-positive upper keratinized cells
Manually annotated by BRENDA team
-
exclusive detection of active enzyme in conditioned medium of dissociated cells, detection of proenzyme only in conditioned medium of non-dissociated cells. Enzyme protein is greatly reduced by treatment with the epidermal growth factor receptor inhibitor AG1478 and the mitogen activated protein kinase kinase inhibitor U0126
Manually annotated by BRENDA team
-
MMP-7 expression analysis semiquantitatively by immunohistochemistry in prostate cancer. E1AF, an ets-oncogene family transcription factor, expression correlates with that of MMP-7
Manually annotated by BRENDA team
-
invasive prostate cancer cells, high enzyme expression level
Manually annotated by BRENDA team
-
presence of enzyme in plasma of normal and azoospermic semen
Manually annotated by BRENDA team
-
induction of enzyme expression by TNF-alpha and interleukin IL-1beta
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
wild-type MMP-7 Gly137 is distributed both in the membrane and cytosol fractions
Manually annotated by BRENDA team
-
pro-MMP-7 is diffusely distributed in epithelial cells of the endometrium, while the mature enzyme is located at the plasma membrane
-
Manually annotated by BRENDA team
additional information
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
human enzyme expressed in COS cells as a latent form which undergoes autocleavage in presence of 4-aminophenylmercuric acetate to a 21000 MW and a 19000 MW active forms
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 19000, human, active form, SDS-PAGE under reducing condition; x * 28000, human, proenzyme, SDS-PAGE under reducing condition
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme
-
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4
-
purified mutants are stable at
50 - 60
-
purified enzyme with or without heparin and cholesterol sulfate, 10 min, 10-40% activity remaining, overview
69 - 76
-
50% of the activity is lost upon incubation at 69C for 10 min, activity decreases to zero as temperature is raised to 76C
70
-
purified enzyme, inactivation within 10 min
additional information
-
in thermal incubation of the enzyme at 50-70C, heparin increases the relative activity (the ratio of kcat/Km of MMP-7 with incubation to that without it), while cholesterol sulfate decreases the relative activity
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
guanidine-HCl
-
half of inactivation induced at 0.8 M
urea
-
half of inactivation induced at 2 M urea
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
fusion protein of glutathione S-transferase and human promatrilysin expressed in Escherichia coli, further activation to matrilysin
-
inactive zymogen is activated: by 4-aminophenylmercuric acetate, yielding an intermediate form of 21000 MW and an active species of 19000 MW, by stromelysin 1 in a single-step mechanism
-
latent precursor purified from transfected mouse myeloma cell conditioned medium, activation by 4-aminophenylmercuric acetate, trypsin and incubation at elevated temperatures
-
recombinant enzyme
-
recombinant enzyme from Escherichia coli
-
recombinant enzyme from Escherichia coli strain BL21(DE3) inclusion bodies, after solubilization and refolding, by gel filtration
-
recombinant solubilized and refolded enzyme from Escherichia coli strain BL21(DE3) inclusion bodies by ammonium sulfate fractionation and heparin affinity chromatography
-
recombinant wild-type and mutant matrilysins, after solubilization from Escherichia coli strain BL21 inclusion bodies, by cation exchange chromatography and gel filtration
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
active MMP-7 lacking the propeptide expressed in Escherichia coli BL21(DE3)
-
catalytic domain expressed in Escherichia coli
-
DNA and amino acid sequence determination, overexpression in Escherichia coli strain BL21(DE3) in inclusion bodies
-
expression analysis
-
expression in Escherichia coli
-
expression in Escherichia coli strain BL21(DE3) in inclusion bodies
-
expression of wild-type and mutant matrilysins in Escherichia coli strain BL21 in inclusion bodies
-
MMP-7 genotyping
-
MMP-7 genotyping in healthy persons and liver cirrhosis patients, overview
-
MMP-7 genotyping, overview
-
overexpression of MMP-7 in Escherichia coli strain BL21(DE3)
-
prepromatrliysin cDNA expressed in Escherichia coli
-
quantitative real time PCR enzyme expression analysis
-
quantitative real-time RT-PCR analysis of MMP-7 in different endometriosis samples
-
recombinant expression of the enzyme in Escherichia coli strain BL21(DE3) in inclusion bodies
-
recombinant pro-matrilysin
-
semi- and quantitative MMP-7 expression analysis in SW620 cells
-
wild-type and mutant matrylysin cDNA in plasmid pUN121 expressed in Escherichia coli BL21(DE3)
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
1,25-dihydroxyvitamin D3, i.e. 1, 25(OH)2D3, significantly reduces the MMP-7 and MMP-9 and increases the TIMP-1 inhibitor level in Mycobacterium tuberculosis antigen stimulated and unstimulated mononuclear cell cultures of pulmonary tunerculosis patients as compared to healthy persons
-
andrographolide diminishes the activity and the mRNA and protein levels of MMP-7, but not MMP-2 or MMP-9. The downregulation of MMP-7 appears to be via the inactivation of activator protein-1, AP-1, overview
-
dominant negative insulin-like growth factor-I receptor, i.e. IGF-IR/dn, suppresses MMP-7 expression in invasive subcutaneous tumors. IGF-stimulated secretion of matrilysin and IGF-IR/dn blocks IGF-mediated matrilysin induction in three gastrointestinal cancers, overview
-
expression of MMP-7 is downregulated by tamoxifen and 5-fluorouracil in combination in HT-29 cells
-
fibulin-5 downregulates MMP-7, suppression of fibulin-5, as well as deletion of its RGD motif, induces MMP-7 expression in lung. Suppression of MMP-7 expression by fibulin-5 is mediated by an integrin-binding RGD motif via the extracellular signal-regulated kinase pathway
-
Helicobacter pylori infection upregulates the expression of matrix metalloproteinases, involved in chronic inflammation, ulceration, and cancer development
-
IGF stimulates matrilysin expression in gastrointestinal cancer cell lines
-
infection by Mycobacterium tuberculosis upregulates MMP-7 expression
-
inhibition of hyaluronan synthases HAS2 and HAS3 highly decreases MMP-7 expression and activity in SW620 cells
-
MMP-7 expression is induced in te epidermis by physiological processes such as wound healing, but also malignant transformation of epidermal cells
-
MMP7 is upregulated by oxaliplatin in colon cancer cell lines. FasL expression is also upregulated by oxaliplatin treatment but decreased in the plasma membrane of resistant cells
-
Mycobacterium tuberculosis infection and its antigen cause an increase in MMP-7 expression in mononuclear cell cultures of pulmonary tunerculosis patients as compared to healthy persons untreated with 1,25-dihydroxyvitamin D3
-
no apparent regulation of the expression of MMP-7 by either tumor necrosis factor or enamel matrix derivative
-
possibly SFRP5 downregulation upregulates MMP-7 via the noncanonical Wnt pathway, overview
-
serum MMP-7 is increased in diabetic renal disease and diabetic diastolic dysfunction
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syndecan-2 enhances both expression and secretion of MMP-7, directly interacts with pro-MMP-7, and potentiates the enzymatic activity of pro-MMP-7 by activating its processing into the active MMP-7. Syndecan-2 functions as a docking receptor for pro-MMP-7 in colon cancer cells, overview
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A15T
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a naturally occuring polymorphism, not involved in liver cirrhosis
E198A
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site-directed mutagenesis
E198C
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site-directed mutagenesis
E198D
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site-directed mutagenesis
E198Q
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site-directed mutagenesis
G137D
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a naturally occuring polymorphism, the Asp137 genetic variant of MMP-7 is susceptible to liver cirrhosis, MMP-7 D137 shows an increased level in its distribution to the plasma membrane of HSCs and an enhanced ability on cell migration, overview. It converts to its active form in specific microdomains
R77H
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a naturally occuring polymorphism, not involved in liver cirrhosis
V470M
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a naturally occuring polymorphism, not involved in liver cirrhosis
Y193F
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site-directed mutagenesis, the mutant shows no pH-dependence shift, as does mutants Y219X
Y216F
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site-directed mutagenesis, the mutant shows no pH-dependence shift, as does mutants Y219X
Y219A
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site-directed mutagenesis, the mutant variant retains its catalytic activity, but exhibits narrower pH-dependence than the wild-type MMP-7
Y219C
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site-directed mutagenesis, the mutant variant retains its catalytic activity, but exhibits narrower pH-dependence than the wild-type MMP-7
Y219D
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site-directed mutagenesis, the mutant variant retains its catalytic activity, but exhibits narrower pH-dependence than the wild-type MMP-7
Y219F
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site-directed mutagenesis, the mutant variant retains its catalytic activity, but exhibits narrower pH-dependence than the wild-type MMP-7
Y219S
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site-directed mutagenesis, the mutant variant retains its catalytic activity, but exhibits narrower pH-dependence than the wild-type MMP-7
additional information
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme from Escherichia coli strain BL21(DE3) inclusion bodies through solubilization by 8 M urea, followed by anion exchange chromatography and dilution to 6 M urea, refolding in 6 M urea, 20 mM Tris-HCl, 10 mM CaCl2, and 100 mM NaCl, pH 7.5, after refolding dialysis in the same buffer with 10 mM ZnCl2, ultrafiltration, overview
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recombinant enzyme, solubilization from Escherichia coli strain BL21(DE3) inclusion bodies by 6 M guanidine HCl, and refolded with 1 M L-arginine
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recombinant MMP-7 from Escherichia coli strain BL21(DE3) inclusion bodies, solubilization and refolding at 1 M L-arginine
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recombinant wild-type and mutant matrilysins from Escherichia coli strain BL21 inclusion bodies dialyzed in 8 M urea containing 50 mM Tris, pH 7.4, 50 mM NaCl, 10 mM CaCl2, 0.1 mM zinc acetate, 0.05% Brij-35, 0.02% NaN3, and 0.01% Triton X-100, followed by gel filtration
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
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method to localize enzyme activity within tissues by selective degradation of crosslinked carboxymethylated transferrin on polyethylene films
diagnostics
drug development
medicine
pharmacology
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MMP-7 is an important target for antimetastasis therapy of colorectal cancer because it is a strong proteolytic factor secreted from the cancer cell itself and it induces tumor angiogenesis