3.4.24.22: stromelysin 2
This is an abbreviated version!
For detailed information about stromelysin 2, go to the full flat file.
Word Map on EC 3.4.24.22
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3.4.24.22
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metalloproteinases
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mmp-9
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collagen
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metastasis
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timps
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endothelial
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stromelysin-1
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gelatinase
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cartilage
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basement
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keratinocytes
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zymography
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matrilysin
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diagnostics
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collagenase-1
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collagenolytic
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medicine
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sdc1
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metalloelastase
- 3.4.24.22
- metalloproteinases
- mmp-9
- collagen
- metastasis
- timps
- endothelial
- stromelysin-1
- gelatinase
- cartilage
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basement
- keratinocytes
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zymography
- matrilysin
- diagnostics
- collagenase-1
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collagenolytic
- medicine
- sdc1
- metalloelastase
Reaction
Similar to stromelysin 1, but action on collagen types III, IV and V is weak =
Synonyms
Matrix metalloproteinase 10, Matrix metalloproteinase-10, MMP-10, MMP10, More, Proteoglycanase 2, ST-2, stromelysin 2, stromelysin-2, Transformation-associated protein 34A, Transin 2, Transins, 2
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3.4.24.22 stromelysin 2Advanced search results
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results (Substrates Products
Substrates Products on EC 3.4.24.22 - stromelysin 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-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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?
Ac-Pro-Leu-Gly-(2-mercapto-4-methyl-pentanoyl)-Leu-Gly-OC2H5 + H2O
?
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?
platelet-derived growth factor receptor alpha + H2O
?
cleavage into two fragments of about 40 and 80 kDa, cleavage site is VPAS416.417ILDL in the extracellular domain
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?
ADAMTS-like protein 1 + H2O
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i.e. punctin-1, an extracellular matrix protein. cooperative processing of ADAMTSL1 by both MMP10 and MMP2, EC 3.4.24.24
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?
ADAMTS-like protein 1 + H2O
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recombinant recombinant human ADAMTSL1 (isoform 1), generation of a 40 kDa N-terminal cleavage fragment, cleavage site is MPYD372.373LYHP
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?
ADAMTS-like protein 1 + H2O
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i.e. punctin-1, an extracellular matrix protein. cooperative processing of ADAMTSL1 by both MMP10 and MMP2, EC 3.4.24.24
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?
ADAMTS-like protein 1 + H2O
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recombinant recombinant human ADAMTSL1 (isoform 1), generation of a 40 kDa N-terminal cleavage fragment, cleavage site is MPYD372.373LYHP
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?
collagen alpha-1(l) + H2O
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cleavage site is GPPG993-/-994LAGP
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?
collagen alpha-2(I) + H2O
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cleavage sites are GPQG871-/-872LLGA, EPGP902-/-903LGIS and GPAG991-/-992SVGP
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?
collagen alpha-2(I) + H2O
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cleavage sites are GPQG871-/-872LLGA, EPGP902-/-903LGIS and GPAG991-/-992SVGP
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?
additional information
?
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participates in activation of procollagenase proMMP-1
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?
additional information
?
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expression of the collagenase gene family, of which the stromelysin-2 gene is one, might play a role in cancer
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?
additional information
?
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cells resistant to protein kinase C potentiated, transcription factor p53 mediated apoptosis express a higher level of matrix metalloproteinases MMP-9 and MMP-10. Matrix metalloproteinases function confers protection from protein kinase C/p53 induced apoptosis and are implicated in tumor cell resistance
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?
additional information
?
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enzyme is involved in intestinal re-epithelialization in vivo and up-regulated by cytokines involved in wound repair
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?
additional information
?
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matrix metalloproteinase MMP-1 zymogen activation by enzyme and other serine proteases is central to endothelial cell-mediated collagen degradation and capillary tube regression in 3D collagen matrices
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?
additional information
?
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active MMP-10 does not cleave collagen type 1 directly, it does activate the collagenase MMP-1, EC 3.4.24.7. The ability of active MMP-10 to superactivate MMP-1 creates a plasmin/MMP-10/MMP-1 proteolytic axis effectively enhances collagen type 1 degradation
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?
additional information
?
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MMP-10 is a potent activator of a number of MMP pro-enzymes, including pro-MMP-1, -7, -8, -9 and -13
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?
additional information
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recombinant MMP-10 decreases integrin alpha3beta1-expression and cell adhesion of SV40-transformed human corneal epithelial cells, overview
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?
additional information
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stromelysins are enzymatically active against proteoglycans, procollagenase, and fibronectin
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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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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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expression of transin and transin-2 in tumor cells might play a role in tumor invasion
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?
