3.4.24.34: neutrophil collagenase
This is an abbreviated version!
For detailed information about neutrophil collagenase, go to the full flat file.
Word Map on EC 3.4.24.34
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3.4.24.34
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mmp-9
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metalloproteinases
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zymography
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metastasis
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timp-1
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endothelial
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angiogenesis
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necrosis
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artery
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fibrosis
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cartilage
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gelatinase
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gelatin
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osteoarthritis
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joint
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periodontal
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tnf
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arthritis
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plaque
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infarct
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vessel
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rheumatoid
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myocardial
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invasiveness
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plasminogen
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basement
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synovial
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chondrocytes
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gingival
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articular
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transwell
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mt1-mmp
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aortic
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aneurysm
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collagenolytic
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aggrecan
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matrigel
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atherosclerotic
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stromelysins
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signal-regulated
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erk
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crevicular
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doxycycline
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gelatinolytic
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matrix-degrading
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anti-invasive
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diagnostics
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disintegrin
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upa
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photoaging
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membrane-type
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medicine
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biotechnology
- 3.4.24.34
- mmp-9
- metalloproteinases
-
zymography
- metastasis
- timp-1
- endothelial
- angiogenesis
- necrosis
- artery
- fibrosis
- cartilage
- gelatinase
- gelatin
- osteoarthritis
- joint
- periodontal
- tnf
- arthritis
- plaque
- infarct
- vessel
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rheumatoid
- myocardial
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invasiveness
- plasminogen
-
basement
- synovial
- chondrocytes
- gingival
-
articular
-
transwell
- mt1-mmp
- aortic
- aneurysm
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collagenolytic
- aggrecan
- matrigel
- atherosclerotic
- stromelysins
-
signal-regulated
- erk
-
crevicular
- doxycycline
-
gelatinolytic
-
matrix-degrading
-
anti-invasive
- diagnostics
-
disintegrin
- upa
-
photoaging
-
membrane-type
- medicine
- biotechnology
Reaction
Cleavage of interstitial collagens in the triple helical domain. Unlike EC 3.4.24.7, interstitial collagenase, this enzyme cleaves type III collagen additional information slowly than type I =
Synonyms
collagenase-2, collagenases-8, EC 3.4.24.7, HNC, human neutrophil collagenase, matrix metalloproteinase, Matrix metalloproteinase 8, Matrix metalloproteinase-8, metalloproteinase-8, MetMMP-8, MMP-7, MMP-8, MMP8, neutrophil collagenase, neutrophil collagenase MMP-8, neutrophil interstitial collagenase, PheMMP-8, PMNL collagenase, PMNL-CL, polymorphonuclear leukocyte collagenase, whMMP-8
ECTree
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Posttranslational Modification
Posttranslational Modification on EC 3.4.24.34 - neutrophil collagenase
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glycoprotein
proteolytic modification
glycoprotein
MMP-8 is secreted as glycosylated zymogen, with a prodomain bound to the metal active site
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recombinant mutant enzymes are purified in the proenzyme form and all display an apparent molecular mass of 79000 Da, 4-aminophenylmercuric acetate-initiated autolytic processing to the fully activated form of the purified mutants, generation of the 59000 Da active enzyme after removal of the propeptide
proteolytic modification
MMP-8 is secreted as glycosylated zymogen, with a prodomain bound to the metal active site. Catalysis is activated by proteolytic cleavage of the prodomain, which exposes the active site