3.4.24.B7: matrix metalloproteinase-26
This is an abbreviated version!
For detailed information about matrix metalloproteinase-26, go to the full flat file.
Word Map on EC 3.4.24.B7
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3.4.24.B7
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endometrial
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timp-4
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mmp-1
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matrilysins
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menstrual
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medicine
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pro-mmp-9
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olomouc
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metalloelastase
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palacky
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metalloproteinase-4
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prodomain
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diagnostics
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synthesis
- 3.4.24.B7
- endometrial
- timp-4
- mmp-1
- matrilysins
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menstrual
- medicine
- pro-mmp-9
-
olomouc
- metalloelastase
-
palacky
-
metalloproteinase-4
- prodomain
- diagnostics
- synthesis
Reaction
proteolytic degradation of proteins =
Synonyms
endometase, endometase/matrilysin-2, M10.029, matrilysin 2, matrilysin-2, matrilysis-2/MMP-26, matrix metalloproteinase-26, metalloproteinases-26, MMP-26, MMP-26/endometase/matrilysin-2, More
ECTree
3.4.24.B7 matrix metalloproteinase-26Advanced search results
results (
results (Inhibitors
Inhibitors on EC 3.4.24.B7 - matrix metalloproteinase-26
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INHIBITOR 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
(3R)-N-hydroxy-2-[(4-methoxyphenyl)sulfonyl]-1,2,3,4-tetrahydroisoquinoline-3-carboxamide
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(3S)-N-hydroxy-2-[(4-methoxyphenyl)sulfonyl]-1,2,3,4-tetrahydroisoquinoline-3-carboxamide
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Brij-35
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optimally activating at 0.056 mM, at concentrations above the critical micelle concentration, it inhibits the enzyme noncompetitively at 0.05%, i.e. 0.417 mM
N-[(2R)-2-(hydroxamidocarbonylmethyl)-4-methylpentanoyl]-L-tryptophan
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i.e. GM6001
SDS
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optimally activating at 0.0095 mM, at concentrations above the critical micelle concentration
Tetradecyltrimethylammonium bromide
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optimally activating at 0.0075 mM, at concentrations above the critical micelle concentration
Triton X-100
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optimally activating at 0.140 mM, at concentrations above the critical micelle concentration
Tween 20
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optimally activating at 0.079 mM, at concentrations above the critical micelle concentration
additional information
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the hydrolytic activity of endometase is detergent concentration dependent, exhibiting a bell-shaped curve with its maximum activity near the critical micelle concentration of nonionic detergents tested, overview. Monomer of detergents may activate and stabilize MMPs to enhance catalysis, but micelle of detergents may sequester enzyme and block the substrate binding site to impede catalysis
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