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Information on EC 3.4.24.17 - stromelysin 1
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3.4.24.17 stromelysin 1Specify your search results
Word Map
- 3.4.24.17
- metalloproteinases
- mmp-1
- cartilage
- arthritis
- joint
- osteoarthritis
-
rheumatoid
- synovial
- chondrocytes
- necrosis
- timps
-
articular
- gelatinase
- tnf
- interleukin-1
- knee
-
zymography
- degeneration
- aggrecan
- proteoglycans
-
c-reactive
-
interstitial
- gelatin
- plasminogen
- proteinases
- cox-2
- synoviocytes
- il-1beta
-
fibroblast-like
-
cruciate
-
intervertebral
- ligament
- matrilysin
- pulposus
-
matrix-degrading
- adamts-4
- synovitis
- thrombospondin
-
intra-articular
-
subchondral
-
emmprin
-
chondroprotective
-
photoaging
- collagenases
- diagnostics
- medicine
- aggrecanase
-
prommp-9
-
neoepitope
-
gelatinolytic
- mt1-mmp
-
collagenolytic
- drug development
- analysis
The enzyme appears in viruses and cellular organisms
Synonyms
mmp-3, stromelysin, matrix metalloproteinase-3, stromelysin-1, matrix metalloproteinase 3, transin, stromelysin 1, proteoglycanase, matrixin, matrix metalloprotease-3, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Collagen-activating protein
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-
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Collagenase activating protein
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-
-
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Matrix metalloproteinase 3
matrix metalloproteinase-3
MMP-3
MMP3
Neutral proteoglycanase
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-
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Procollagenase activator
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-
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Proteoglycanase
PTR1 protein
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-
-
-
Stromelysin
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-
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stromelysin-1
Transin
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-
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Matrix metalloproteinase 3
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-
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matrix metalloproteinase-3
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MMP-3
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-
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MMP-3
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Proteoglycanase
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-
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-
stromelysin-1
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-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
preferential cleavage where P1', P2' and P3' are hydrophobic residues
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-
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
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-
-
-
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CAS REGISTRY NUMBER
COMMENTARY
79955-99-0
-
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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-Arg-Pro-Lys-Pro-Tyr-Ala-norvaline-Trp-Met-Lys(2,4-dinitrophenyl)-NH2 + H2O
?
-
hydrolyzed 60 times more rapidly by metalloproteinase-3 than metalloproteinase-1, little discrimination between metalloproteinase-3 and metalloproteinase-2
-
-
?
(7-Methoxycoumarin-4-yl)acetyl-Arg-Pro-Lys-Pro-Val-Glu-norvaline-Trp-Arg-Lys(2,4-dinitrophenyl)-NH2 + H2O
(7-Methoxycoumarin-4-yl)acetyl-Arg-Pro-Lys-Pro-Val-Glu + norvaline-Trp-Arg-Lys(2,4-dinitrophenyl)-NH2
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-
-
?
(7-Methoxycoumarin-4-yl)acetyl-Arg-Pro-Lys-Pro-Val-Glu-norvaline-Trp-Arg-Lys(2,4-dinitrophenyl)-NH2 + H2O
?
-
a fluorogenic substrate selectively hydrolyzed by stromelysin 1
-
-
?
(7-methoxycoumarin-4-yl)acetyl-P-L-G-L-(L)-2,3-diaminopropionylamide-A-R + H2O
?
-
-
-
?
(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-Lys-Pro-Gln-Gln-Phe-Phe-Gly-Leu-Lys-(2,4-dinitrophenyl)-Gly + H2O
?
-
hydrolyzed equally well by metalloproteinase-3 and metalloproteinase-2, metalloproteinase-1 shows 25% of the activity compared to metalloproteinase-3
-
-
?
2,4-Dinitrophenyl-Arg-Pro-Lys-Pro-Leu-Ala-norvaline-Trp-NH2 + H2O
2,4-Dinitrophenyl-Arg-Pro-Lys-Pro-Leu-Ala + norvaline-Trp-NH2
-
-
-
?
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-Tyr-Ala-Tyr-Trp-Met-Arg-NH2 + H2O
2,4-Dinitrophenyl-Pro-Tyr-Ala + Tyr-Trp-Met-Arg-NH2
6-[(7-nitro-2,1,3-benzoxadiazol-4-yl)amino]hexanoy-L-Arg-L-Pro-L-Lys-L-Pro-L-Leu-L-Ala-L-Nva-L-Trp-L-Lys(7-dimethylaminocoumarin-4-yl)-NH2 + H2O
?
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-
-
-
?
acetyl-Pro-Leu-Gly-[2-mercapto-4-methyl-pentanoyl]-Leu-Gly-OC2H5 + H2O
?
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-
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-
?
Antithrombin III + H2O
?
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cleavage of the P1-P1' bond in the reactive center
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-
?
Fibronectin + H2O
Intact fibronectin subunit MW 22000 + a disulfide-bonded COOH-terminal MW 20000 polypeptide
Mca-Arg-Pro-Lys-Pro-Val-Glu-Nva-Trp-Arg-Lys(Dnp)-NH2 + H2O
?
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fluorogenic substrate
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-
?
2,4-Dinitrophenyl-Pro-Tyr-Ala-Tyr-Trp-Met-Arg-NH2 + H2O
2,4-Dinitrophenyl-Pro-Tyr-Ala + Tyr-Trp-Met-Arg-NH2
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-
-
-
?
2,4-Dinitrophenyl-Pro-Tyr-Ala-Tyr-Trp-Met-Arg-NH2 + H2O
2,4-Dinitrophenyl-Pro-Tyr-Ala + Tyr-Trp-Met-Arg-NH2
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-
-
?
alpha-Proteinase inhibitor + H2O
2,4-Dinitrophenyl-Pro-Leu-Gly + Ile-Ala-Gly-Arg-NH2
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alpha1-proteinase inhibitor, cleavage within the reactive site loop
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-
?
alpha-Proteinase inhibitor + H2O
2,4-Dinitrophenyl-Pro-Leu-Gly + Ile-Ala-Gly-Arg-NH2
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?
cytosolic protein Apaf-1 + H2O
?
the 130 kD full-length Apaf-1 is truncated to about 37 kD and 20 kD proteins
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-
?
Fibronectin + H2O
Intact fibronectin subunit MW 22000 + a disulfide-bonded COOH-terminal MW 20000 polypeptide
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?
Fibronectin + H2O
Intact fibronectin subunit MW 22000 + a disulfide-bonded COOH-terminal MW 20000 polypeptide
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?
Fibronectin + H2O
Intact fibronectin subunit MW 22000 + a disulfide-bonded COOH-terminal MW 20000 polypeptide
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?
Laminin + H2O
?
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cleavage activity is barely detected as a much lower activity as reported
-
?
pro-caspase-9 + H2O
active caspase-9 + caspase-9 propeptide
activation
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-
?
pro-caspase-9 + H2O
active caspase-9 + caspase-9 propeptide
an additional cytosolic protein, possibly Apaf-1, is required for activation, rat substrate
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-
?
Collagen type IV + H2O
additional information
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4 major fragments of MW 165000, 145000, 125000 and 110000
?
Collagen type IV + H2O
additional information
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no degradation of type I collagen
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?
Collagen type IV + H2O
additional information
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limited activity
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?
additional information
?
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enzyme is secreted from the cells as an inactive zymogen
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?
additional information
?
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degrades a number of extracellular matrix components
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?
additional information
?
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participates in activation of procollagenases and progelatinase B
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?
additional information
?
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enzyme is secreted from the cells as an inactive zymogen
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?
additional information
?
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degrades a number of extracellular matrix components
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?
additional information
?
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participates in activation of procollagenases and progelatinase B
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?
additional information
?
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may play a role in the normal turnover of the connective tissue matrix as well as in the joint destruction of chronic synovitis
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?
additional information
?
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believed to play a role in pathological conditions such as arthritis and tumor invasion
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?
additional information
?
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degrading all of the major macromolecules of the extracellular matrix
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?
additional information
?
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required for the degradation of extracellular matrix components during normal embryo development, morphogenesis and tissue remodelling
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?
additional information
?
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stromelysin (MMP3), through its action on collagen and other matrix metalloproteinases, influences arterial wall remodeling
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?
additional information
?
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matrix metalloproteinases are endopeptidases capable of cleaving various components of extracellular matrix
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?
additional information
?
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the enzyme degrades a variety of extracellular matrix proteins, including collagen types III-V and fibronectin, and also activate other proteases, including MMP-1, MMP-7, MMP-8, and MMP-9
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-
?
additional information
?
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the enzyme degrades a variety of extracellular matrix proteins, including collagen types III-V and fibronectin, and also activate other proteases, including MMP-1, MMP-7, MMP-8, and MMP-9
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?
additional information
?
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the enzyme degrades several dentin matrix proteins, a demineralized and pretreated dentin block is used for activity assays. Enzyme MMP-3 is capable of degrading the protein core of proteoglycans, resulting in the release of soluble glycosaminoglycans
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?
additional information
?
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enzyme attacks the basal lamina and tight junction proteins, opening the blood-brain barrier and thereby facilitating neutrophil influx
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?
additional information
?
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enzyme is expressed as a protective response and plays an important role in host defense during squamous cell carcinoma tumorigenesis
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?
additional information
?
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genetic ablation of MMP-3 does not significantly affect tumor growth and metastasis in the MMTV-PyMT model
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?
additional information
?
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MMPs belong to a family of over 20 neutral endopeptidases that are collectively able to cleave all extracellular matrix components as well as many non-extracellular matrix proteins. The stromelysins, MMP-3, MMP-10 and MMP-11, have a domain arrangement similar to that of collagenases, but they do not cleave interstitial collagens
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?
additional information
?
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degradation of glomerular basement membrane
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-
?
additional information
?
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enzyme is secreted from the cells as an inactive zymogen
-
-
?
additional information
?
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-
degrades a number of extracellular matrix components
-
-
?
additional information
?
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-
participates in activation of procollagenases and progelatinase B
-
-
?
additional information
?
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cleavage at multiple chondroitin sulfate-binding sites along the protein core
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-
?
additional information
?
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glomerular basement membrane degradation by glomeruli may be attributable to stromelysin and suggest an important role for these proteinases in glomerular pathophysiology
-
-
?
additional information
?
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enzyme is secreted from the cells as an inactive zymogen
-
-
?
additional information
?
-
-
degrades a number of extracellular matrix components
-
-
?
additional information
?
-
-
participates in activation of procollagenases and progelatinase B
-
-
?
Proteoglycan + H2O
additional information
-
-
cartilage
degradation to 12.0 S fragments by the HMW form and 10.3 S fragments by the KMW enzyme
?
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NATURAL SUBSTRATE
NATURAL 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
pro-caspase-9 + H2O
active caspase-9 + caspase-9 propeptide
activation
-
-
?
additional information
?
-
-
may play a role in the normal turnover of the connective tissue matrix as well as in the joint destruction of chronic synovitis
-
-
?
additional information
?
-
-
believed to play a role in pathological conditions such as arthritis and tumor invasion
-
-
?
additional information
?
-
-
degrading all of the major macromolecules of the extracellular matrix
-
?
additional information
?
-
-
required for the degradation of extracellular matrix components during normal embryo development, morphogenesis and tissue remodelling
-
?
additional information
?
-
-
stromelysin (MMP3), through its action on collagen and other matrix metalloproteinases, influences arterial wall remodeling
-
-
?
additional information
?
-
-
matrix metalloproteinases are endopeptidases capable of cleaving various components of extracellular matrix
-
-
?
additional information
?
-
the enzyme degrades a variety of extracellular matrix proteins, including collagen types III-V and fibronectin, and also activate other proteases, including MMP-1, MMP-7, MMP-8, and MMP-9
-
-
?
additional information
?
-
-
the enzyme degrades a variety of extracellular matrix proteins, including collagen types III-V and fibronectin, and also activate other proteases, including MMP-1, MMP-7, MMP-8, and MMP-9