3.4.24.17: stromelysin 1
This is an abbreviated version!
For detailed information about stromelysin 1, go to the full flat file.
Word Map on EC 3.4.24.17
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3.4.24.17
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metalloproteinases
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mmp-1
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cartilage
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arthritis
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joint
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osteoarthritis
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rheumatoid
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synovial
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chondrocytes
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necrosis
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timps
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articular
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gelatinase
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tnf
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interleukin-1
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knee
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zymography
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degeneration
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aggrecan
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proteoglycans
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c-reactive
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interstitial
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gelatin
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plasminogen
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proteinases
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cox-2
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synoviocytes
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il-1beta
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fibroblast-like
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cruciate
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intervertebral
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ligament
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matrilysin
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pulposus
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matrix-degrading
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adamts-4
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synovitis
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thrombospondin
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intra-articular
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subchondral
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emmprin
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chondroprotective
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photoaging
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collagenases
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diagnostics
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medicine
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aggrecanase
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prommp-9
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neoepitope
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gelatinolytic
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mt1-mmp
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collagenolytic
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drug development
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analysis
- 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
Reaction
preferential cleavage where P1', P2' and P3' are hydrophobic residues =
Synonyms
Collagen-activating protein, Collagenase activating protein, matrix metalloprotease-3, Matrix metalloproteinase 3, matrix metalloproteinase-3, matrixin, MMP-3, MMP3, Neutral proteoglycanase, Procollagenase activator, Proteoglycanase, PTR1 protein, ST1, Stromelysin, stromelysin-1, Transin
ECTree
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Metals Ions
Metals Ions on EC 3.4.24.17 - stromelysin 1
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Ca2+
Co2+
Mn2+
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addition of 5 mM Mn2+ in the presence of Ca2+ restores activity of the apoenzyme, not by Mn2+ alone
Zinc
Zn2+
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Ca2+ is required to maintain the active conformation of the enzyme, full activity is detected at 1 mM Ca2+, at pH 7.5 and is retained at even higher concentrations of Ca2+, at lower concentrations the enzyme is autolyzed
Ca2+
-
removal of Ca2+ from the enzyme solution results in a complete loss of activity that can be fully restored by addition of 1 mM Ca2+
Ca2+
-
Ca2+ is required to maintain the active conformation of the enzyme, full activity is detected at 1 mM Ca2+, at pH 7.5 and is retained at even higher concentrations of Ca2+, at lower concentrations the enzyme is autolyzed
Ca2+
-
Ca2+ is required to maintain the active conformation of the enzyme, full activity is detected at 1 mM Ca2+, at pH 7.5 and is retained at even higher concentrations of Ca2+, at lower concentrations the enzyme is autolyzed
Ca2+
-
Ca2+ is required to maintain the active conformation of the enzyme, full activity is detected at 1 mM Ca2+, at pH 7.5 and is retained at even higher concentrations of Ca2+, at lower concentrations the enzyme is autolyzed
-
addition of 0.5 mM Co2+ in the presence of Ca2+ restores activity of the apoenzyme, not by Co2+ alone
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proenzyme and mature active form contain nearly 2 mol of Zn/mol of protein, location at the active site, zinc-cysteine interaction is required for the preservation of latency
Zinc
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Zn2+: addition of 0.5 mM Zn2+ in the presence of Ca2+ restores activity of the apoenzyme, not by Zn2+ alone
Zinc
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zinc metalloprotein, proenzyme contains two Zn2+, the Zn2+ at the active site is bound to His-201, His-205, and His-211 and Cys-75 in the propeptide
Zn2+
modeling of stromelysin-1 binding biphenol moiety in the S1' pocket and acetohydroxamic acid chelating catalytic zinc