3.4.24.B4: matrix metalloproteinase-13
This is an abbreviated version!
For detailed information about matrix metalloproteinase-13, go to the full flat file.
Word Map on EC 3.4.24.B4
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3.4.24.B4
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cartilage
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chondrocytes
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osteoarthritis
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metalloproteinases
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joint
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articular
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aggrecan
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degeneration
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mmp-2
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tnf
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knee
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timp-1
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arthritis
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synovial
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interleukin-1
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proteoglycans
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degener
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cox-2
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osteoblast
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adamts-5
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ligament
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intra-articular
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collagenases
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col2a1
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thrombospondin
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pulposus
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runx2
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cruciate
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zymography
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chondrogenic
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gelatinase
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meniscus
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intervertebral
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subchondral
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disintegrin
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endochondral
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safranin
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synoviocytes
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collagenolytic
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matrix-degrading
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chondroprotective
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ossification
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temporomandibular
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mt1-mmp
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chondrogenesis
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medicine
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stromelysin-1
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diagnostics
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cartilage-specific
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condylar
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analysis
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osteophyte
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drug development
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aggrecanase
- 3.4.24.B4
- cartilage
- chondrocytes
- osteoarthritis
- metalloproteinases
- joint
-
articular
- aggrecan
- degeneration
- mmp-2
- tnf
- knee
- timp-1
- arthritis
- synovial
- interleukin-1
- proteoglycans
-
degener
- cox-2
- osteoblast
- adamts-5
- ligament
-
intra-articular
- collagenases
-
col2a1
- thrombospondin
- pulposus
- runx2
-
cruciate
-
zymography
-
chondrogenic
- gelatinase
- meniscus
-
intervertebral
-
subchondral
-
disintegrin
-
endochondral
-
safranin
- synoviocytes
-
collagenolytic
-
matrix-degrading
-
chondroprotective
-
ossification
-
temporomandibular
- mt1-mmp
-
chondrogenesis
- medicine
- stromelysin-1
- diagnostics
-
cartilage-specific
-
condylar
- analysis
- osteophyte
- drug development
- aggrecanase
Reaction
proteolytic degradation of proteins =
Synonyms
collagenase, collagenase 3, collagenase-3, M10.013, matrix metalloproteinase 13, matrix metalloproteinase-13, MMP-13, MMP13, MMP13a, More, UMRCASE
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Posttranslational Modification
Posttranslational Modification on EC 3.4.24.B4 - matrix metalloproteinase-13
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proteolytic modification
proteolytic modification
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autoproteolysis resulting in two N-glycosylated 29 kDa fragments and one 27 kDa fragment, processing of enzyme proform via a short-living intermediate form to the active form with Tyr85 at its N-terminus
proteolytic modification
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cleavage by trypsin is not effective, processing of the 60 kDa procollagenase 3 by stromelysin or by p-aminophenylmercuric acetate to form an intermediate of 50 kDa, further processing by cleavage of the peptide bond Glu84-Tyr85 resuls in the active 48 kDa mature form, overview
proteolytic modification
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stromelysin-1 can activate the enzyme by cleavage of the Glu57-Leu58 bond of the proform resulting in formation of an intermediate of 50 kDa which is further processed to the 48 kDa active mature form, inactive proform can be activated in 3 different ways: 1. autoproteolytically, 2. via cleavage by several other matrix metalloproteases, 3. in a three-step process using aminophenylmercuric acetate
proteolytic modification
the prodomain of MMP13 determines autoactivation of MMP13 and intracellular degradation of MMP13
proteolytic modification
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the prodomain of MMP13 determines autoactivation of MMP13 and intracellular degradation of MMP13