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Information on EC 3.4.24.23 - matrilysin
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3.4.24.23 matrilysinSpecify your search results
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- 3.4.24.23
- metalloproteinases
- mmp-2
- metastasis
- timp-1
- colorectal
- fibrosis
- collagen
- endothelial
- node
- gelatinase
- e-cadherin
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clinicopathological
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zymography
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interstitial
- gastric
- epithelium
- tumour
- adenocarcinoma
- pulmonary
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basement
- prostate
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invasiveness
- tumorigenesis
- beta-catenin
- gelatin
- carcinogenesis
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resect
- mt1-mmp
- cyclin
- c-myc
- adenoma
- plasminogen
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transwell
- osteopontin
- metalloelastase
- stromelysin-1
- laminin-5
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hemopexin-like
- pharmacology
- upa
- drug development
- alpha-defensins
- collagenase-3
- analysis
- medicine
- diagnostics
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gelatinolytic
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matrix-degrading
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paneth
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membrane-type
The enzyme appears in viruses and cellular organisms
Reaction Schemes
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)
Synonyms
mmp-7, matrilysin, matrix metalloproteinase-7, matrix metalloproteinase 7, matrin, pump-1, matrix metallopeptidase 7, metalloproteinase-7, matrilysin-1, mmp 7, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
matrilysin
matrilysin-1
Matrin
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matrix metalloprotease-7
Matrix metalloproteinase 7
Matrix metalloproteinase pump 1
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Matrix metalloproteinase-7
MMP
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MMP 7
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MMP-7
MMP7
Proteinase, metallo-, pump-1
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Proteinase, PUMP-1
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PUMP
Pump-1 protease
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Putative (or punctuated) metalloproteinase-1
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Putative metalloproteinase
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Uterine metalloendopeptidase
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Uterine metalloproteinase
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additional information
the enzyme belongs to the zinc-dependent endopeptidases
Matrix metalloproteinase 7
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Matrix metalloproteinase 7
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Matrix metalloproteinase-7
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Matrix metalloproteinase-7
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Matrix metalloproteinase-7
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MMP-7
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638796, 649827, 651772, 651777, 651781, 651804, 652071, 652723, 706943, 707003, 707186, 707870, 707880, 707905, 707957, 707986, 708011, 708021, 708084, 708164, 708198, 708293, 708301, 708308, 708392, 708635, 708642, 708667, 708674, 708772, 709079, 709318, 709345, 709415, 709655, 709669, 709809, 710176, 710179, 710651, 710683, 710694, 717204, 717292, 717397, 717399, 717745, 717801, 718394, 754942, 755514
MMP-7
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PUMP
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REACTION
REACTION DIAGRAM
COMMENTARY
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)
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
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CAS REGISTRY NUMBER
COMMENTARY
141256-52-2
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(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
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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
?
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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
?
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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
?
(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
?
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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
?
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MOCAc-PLGL(Dpa)AR
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?
(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
?
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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
(7-methoxycoumarin-4-yl)acetyl-Pro-Leu-Gly + Leu-N-3(2,4-dinitrophenyl)-L-2,3-diaminopropionyl-Ala-Arg-NH2
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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
?
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?
2,4-Dinitrophenyl-Arg-Pro-Leu-Ala-Leu-Trp-Arg-Ser + H2O
?
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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
7-amino-4-methylcoumaryl-Pro-Lys-Pro-Leu-Ala-Leu-Dap(Dnp)-Ala-Arg-NH2 + H2O
?
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?
7-methoxycoumarin-4acetylPLGL(L-2,3-diaminopropionyl)AR + H2O
7-methoxycoumarin-4acetyl-PLG + ?
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?
alpha1-antitrypsin + H2O
?
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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
?
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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
?
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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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?
C-type lectin domain family 3 member A + H2O
?
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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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?
Cy5.5-M7 peptide + H2O
?
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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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?
E-cadherin + H2O
modified E-cadherin + E-cadherin ectodomain
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matrilysin cleaves E-cadherin in its juxtamembrane stalk releasing the entire ectodomain
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?
entactin + H2O
peptide fragment ranging from 29000 to 115000 MW
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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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?
heparin-binding epidermal growth factor precursor + H2O
heparin-binding epidermal growth factor + HB-EGF pro-peptide
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?
Insulin B-chain + H2O
?
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cleavage at 2 points: Ala14-Leu15 and Tyr16-Leu17
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?
laminin-5/Laminin-322 + H2O
90 kDa beta3 chain fragment + ?
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 + ?
i.e. LN5, specific proteolysis by MMP7 in the beta3 chain at Ala515-Ile516, overview
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?
PB-M7vis + H2O
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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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?
pro-alpha-defensin-1 + H2O
alpha-defensin-1 + alpha-defensin-1 propeptide
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i.e. procryptdins
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?
Pro-matrix metalloproteinase 1 + H2O
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activation by specific cleavage at the Gln80-Phe81 bond
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?
proADAM28s + H2O
ADAM28s + propeptide
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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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?
(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
?
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MOCAc-PLGL(Dpa)AR
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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
?
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MOCAc-PLGL(Dpa)AR, Lot 480429
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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
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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
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?
elastin + H2O
elastin peptides
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degradation. MMP-7 mainly cleaves in N- and C-terminal regions of elastin's precursor, which involves linkages in domains encoded by exons 2, 3, 5-7, 26, and 30-33. Only few cleavages occur in the central part of the precursor and no cleavages in regions in elastin that are involved in cross-linking. MMP-7 shows a strong preference for Leu in P1' and also accepts Val, Gly, and Pro at this position, whereas Ala is not preferred at P1', molecular modeling, overview. Not only the size of the amino acid residue in P1' but also the orientation of the neighboring P1 residue and, thus, the orientation of the peptide bond that is cleaved influences the cleavage preference of MMP-7, cleavage site specificity of MMP-7 in human skin elastin, overview
in the range of 500-8000 Da
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?
Fibronectin + H2O
?
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also MMP-7-catalyzed cleavages of chymotryptic fragments of fibronectin by cell-bound MMP-7, overview
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?
Gelatin + H2O
?
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digests the alpha2(I) chain of gelatin in preference to the alpha1(I) chain
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?
Gelatin + H2O
?
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cleaves the alpha2(I) chain of rat gelatin producing major cuts at Gly713-Ile714, Gly775-Leu776, Gly809-Ile810
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?