Information on EC 3.4.24.23 - matrilysin

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.4.24.23
-
RECOMMENDED NAME
GeneOntology No.
matrilysin
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
Cleavage of Ala14-/-Leu and Tyr16-/-Leu in B chain of insulin. No action on collagen types I, II, IV, V. Cleaves gelatin chain alpha2(I) > alpha1(I)
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
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CAS REGISTRY NUMBER
COMMENTARY hide
141256-52-2
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Chinese black-boned sheep and Chinese common sheep
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Manually annotated by BRENDA team
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
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-
-
-
?
(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
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-
-
?
(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
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-
-
?
(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
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MOCAc-PLGL(Dpa)AR
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?
(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
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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
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?
(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
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?
2,4-Dinitrophenyl-Arg-Pro-Leu-Ala-Leu-Trp-Arg-Ser + H2O
?
show the reaction diagram
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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
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?
7-methoxycoumarin-4acetylPLGL(L-2,3-diaminopropionyl)AR + H2O
7-methoxycoumarin-4acetyl-PLG + ?
show the reaction diagram
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?
7-methoxycoumarin-4acetylPLGL(L-2,3-diaminopropionyl)AR + H2O
?
show the reaction diagram
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?
aggrecan + H2O
?
show the reaction diagram
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?
alpha1-antitrypsin + H2O
?
show the reaction diagram
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a single cleavage at the Phe352-Leu353 peptide bond, a locus within active-site loop produces 2 fragments of approximately 50000 MW and 4000 MW
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alpha1PI + H2O
?
show the reaction diagram
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protein, inhibitor of elastase, inactivation by cleavage of Pro357-Met358 peptide bond of its reactive centre
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annexin II + H2O
?
show the reaction diagram
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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
bovine carboxymethylated-transferrin + H2O
?
show the reaction diagram
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?
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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?
casein + H2O
?
show the reaction diagram
Collagen + H2O
?
show the reaction diagram
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?
collagen type IV + H2O
?
show the reaction diagram
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?
connexin-43 + 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
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synthetic fluorescent peptide
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?
decorin + H2O
transforming growth factor-beta + ?
show the reaction diagram
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?
Dinitrophenyl-Pro-Leu-Gly-Ile-Ala-Gly-Pro-D-Arg + H2O
?
show the reaction diagram
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E-cadherin + H2O
modified E-cadherin + E-cadherin ectodomain
show the reaction diagram
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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
entactin + H2O
peptide fragment ranging from 29000 to 115000 MW
show the reaction diagram
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basement membrane protein which bridges laminin and type IV collagen, enzyme produces multiple but distict cleavages in entactin resulting in peptide fragments ranging from 29000 to 115000 MW, cleavage sites: Glu34-Leu35, Gly275-Leu276, Ala637-Leu638, Cys747-Ile748
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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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?
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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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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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 B-chain + H2O
?
show the reaction diagram
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cleavage at 2 points: Ala14-Leu15 and Tyr16-Leu17
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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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?
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
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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
Notch-1 + H2O
?
show the reaction diagram
osteopontin + H2O
?
show the reaction diagram
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?
Oxidized alpha1PI + H2O
?
show the reaction diagram
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cleavage of Phe352-Leu353 bond
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PB-M7vis + H2O
?
show the reaction diagram
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fluorogenic substrate based on a polyamino amino dendrimer core of 14.2 kDa covalently coupled with an fluorescein-labeled peptide fluorescein(aminohexanoic acid)RPLALWRS(aminohexanoic acid)Cand with tetramethylrhodamine
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?
perlecan + H2O
?
show the reaction diagram
pig gelatin type A + H2O
?
show the reaction diagram
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?
pro-alpha-defensin + H2O
alpha-defensin + alpha-defensin propeptide
show the reaction diagram
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?
pro-alpha-defensin-1 + H2O
alpha-defensin-1 + alpha-defensin-1 propeptide
show the reaction diagram
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i.e. procryptdins
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?
pro-beta-defensin + H2O
beta-defensin + beta-defensin propeptide
show the reaction diagram
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?
pro-HNP-1 + H2O
HNP-1 + HNP-1 propeptide
show the reaction diagram
Pro-matrix metalloproteinase 1 + H2O
?
show the reaction diagram
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activation by specific cleavage at the Gln80-Phe81 bond
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proADAM28s + H2O
ADAM28s + propeptide
show the reaction diagram
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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
tenascin-C + H2O
?
show the reaction diagram
-
production of protein fragments
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?
tumor-associated antigen 90K + H2O
?
show the reaction diagram
type IV basement membrane collagen + H2O
?
show the reaction diagram
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?
Type IV collagen + H2O
?
show the reaction diagram
additional information
?
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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
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?
Collagen + H2O
?
show the reaction diagram
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?
connexin-43 + H2O
?
show the reaction diagram
Q10738
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?
E-cadherin + H2O
modified E-cadherin + E-cadherin ectodomain
show the reaction diagram
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matrilysin cleaves E-cadherin in its juxtamembrane stalk releasing the entire ectodomain
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?
elastin + H2O
elastin peptides
show the reaction diagram
-
degradation
in the range of 500-8000 Da
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?
fibronactin + H2O
fibronectin peptide fragments
show the reaction diagram
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MWs of 30 to 175 kDa
-
?
Fibronectin + H2O
?
show the reaction diagram
IGFBP-3 + H2O
?
show the reaction diagram
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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
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?
insulin-like growth factor binding protein-2 + H2O
?
show the reaction diagram
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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
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in the medium of gastric myofibroblasts, knockdown of IGFBP-5 abolished the myofibroblast proliferation response to MMP-7, overview
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?
laminin-332 + H2O
?
show the reaction diagram
-
pericellular substrate
-
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?
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
Notch-1 + H2O
?
show the reaction diagram
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
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?
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
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?
syndecan-2 + H2O
?
show the reaction diagram
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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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?
tenascin-C + H2O
?
show the reaction diagram
-
production of protein fragments
-
-
?
tumor-associated antigen 90K + H2O
?
show the reaction diagram
-
-
-
-
?
Type IV collagen + H2O
?
show the reaction diagram
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?
additional information
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
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partial activation
NaCl
-
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
Sr2+
-
partial activation
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(-)-5-hydroxypluviatolide
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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
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1,10-phenanthroline
1-(4-methoxyphenyl)sulfonyl-4-(tert-butoxycarbonyl)-piperazine-2-carboxylic acid
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1-butanol
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2-butanol
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2-methyl-1-propanol
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2-methyl-2-butanol
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2-Methyl-2-propanol
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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
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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
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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
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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
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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
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-
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
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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
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-
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
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-
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
BB-94
-
[4-(N-hydroxyamino)-(2R)-isobutyl-(3S)-(thienylthiomethyl)-succinyl]-L-Phe-N-methylamine
Brij-35
-
activates MMP-7 in a broad concentration range, but inhibits at high concentration
carboxylate
-
-
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
-
-
Ovostatin
-
-
-
Pseudopeptide inhibitors
-
-
-
R-94138
-
-
RRS269
-
-
Sulfatide
-
associates with the enzyme at the cell surface and inhibits by 80%
Sulfodiimine
-
-
sulindac
-
in sulindac-treated ApcMin/+ mice, a genetic model of human familial adenomatous polyposis, collagen genes, viz. Col1a2, Col5a2, Col6a2, and Col6a3, are upregulated, and matrilysin matrix metalloproteases-7 is downregulated. Mmp7 is found in hot spot areas within the tumors of ApcMin/+ mice treated with the vehicle, but is greatly diminished in those mice treated with sulindac
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
-
i.e. TIMP-1. TIMP-1 and matrilysin co-localize and co-immunoprecipitate in wounded primary airway epithelial cultures. TIMP-1-deficient cultures migrate faster, and epithelial cells spread to a greater extent compared with wild-type cultures. TIMP-1 also inhibits matrilysin-mediated cell migration and spreading in vitro. In vivo, TIMP-1 deficiency enhances airway re-epithelialization after naphthalene injury. TIMP-1 and matrilysin co-localize in airway epithelial cells adjacent to the wound edge
-
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
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
0.00089
entactin
-
-
-
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
-
-
0.0005
PB-M7vis
-
25C, pH 7.4
-
additional information
additional information
-
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
Homo sapiens
-
-
3.5
2,4-dinitrophenyl-Pro-Leu-Gly-Leu-Trp-Ala-D-Arg
Homo sapiens
-
-
0.00051 - 6.08
dansyl-PLALWAR
0.472
Gly-Pro-Gln-Ala-Ile-Ala-Gly-Gln
Homo sapiens
-
-
0.222
Gly-Pro-Gln-Gly-Ile-Ala-Gly-Gln
Homo sapiens
-
-
1.17
Gly-Pro-Gln-Gly-Ile-Ala-Met-Gln
Homo sapiens
-
-
2.47
Gly-Pro-Gln-Gly-Leu-Ala-Gly-Gln
Homo sapiens
-
-
1.92
Gly-Pro-Met-Gly-Ile-Ala-Gly-Gln
Homo sapiens
-
-
additional information
additional information
-
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
5874
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
-
azocoll, proteoglycan
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
5.5 - 8.8
-
5.5: about 30% of activity maximum, 8.8: about 40% of activity maximum
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
-
infiltrating
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