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
-
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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KM Value
KM Value on EC 3.4.24.17 - stromelysin 1
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0.066
(7-Methoxycoumarin-4-yl)acetyl-Arg-Pro-Lys-Pro-Tyr-Ala-norvaline-Trp-Met-Lys(2,4-dinitrophenyl)-NH2
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-
0.025
(7-Methoxycoumarin-4-yl)acetyl-Arg-Pro-Lys-Pro-Val-Glu-norvaline-Trp-Arg-Lys(2,4-dinitrophenyl)-NH2
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-
0.05
(7-Methoxycoumarin-4-yl)acetyl-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly-Leu-Lys-(2,4-dinitrophenyl)-Gly
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-
0.395
acetyl-Pro-Leu-Gly-[2-mercapto-4-methyl-pentanoyl]-Leu-Gly-OC2H5
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pH 6.0, 25°C, catalytic domain (residues 83-247)
additional information
additional information
thermodynamic additivity analysis using stromelysin-1 and a series of biphenyl hydroxamate ligands identified through fragment additivity, thermodynamics determined by isothermal titration calorimetry, corrected for proton transfer events, overview. Additivity arises from enthalpic effects, while interaction entropies are unfavorable, the thermodynamic behavior is masked by proton transfer
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0.9
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wild-type enzyme form
1.4
Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly-Leu-norleucine-NH2
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truncated enzyme form