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
-
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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Inhibitors
Inhibitors on EC 3.4.24.22 - stromelysin 2
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N-isobutyl-N-(4-methoxy-phenylsulfonyl)glycyl hydroxamic acid
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i.e. NNGH, study of binding mode. Interaction of inhibitor with Zn1 atom and S1 subsite
PAI-1
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functions as an upstream regulator of a MMP-10-initiated collagenolytic phenotype, it blocks conversion of MMP-10 to its active form. Neutralization of endogenous PAI-1 with function blocking antibodies accelerates both collagenolysis and activation of MMP-10
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tissue inhibitor of metalloproteinases 1
TIMP-1, the protein is expressed in HEK 293E cells, enzyme binding structure analysis and mechanism of inhibition, detailed overview and comparison to stromelysin-1, EC 3.4.24.17
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additional information
the endogenous tissue inhibitors of metalloproteinases (TIMPs) regulate proteolytic activity by binding tightly to the MMP active site. While each of the four TIMPs can inhibit most MMPs, binding data reveal tremendous heterogeneity in affinities of different TIMP/MMP pairs. Identification of a group of highly conserved contacts at the heart of MMP/TIMP complexes that define the conserved mechanism of inhibition, as well as a second category of diverse adventitious contacts at the periphery of the interfaces
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TIMP-1
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TIMP-1 from brain is upregulated in in the infarcted tissue compared to healthy control areas, overview
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TIMP-2, the protein is expressed in HEK 293E cells
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tissue inhibitor of metalloproteinases 2
TIMP-2, conserved mechanism of inhibition, interactions and conformation analysis, and structural changes induced by complex formation with the enzyme's catalytic domain, detailed overview
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