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
-
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
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Engineering
Engineering on EC 3.4.24.B7 - matrix metalloproteinase-26
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D114A
D165A
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very low rates of hydrolysis that are less than 5% of that seen for wild-type MMP-26
E191A
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very low rates of hydrolysis that are less than 5% of that seen for wild-type MMP-26
H81R
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mutation restores the conventional cysteine-switch in the prodomain but fails to induce the cysteine-swich activation
K189E
V184D
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mutant enzyme shows high rates of fluorescent synthetic peptide hydrolysis
additional information
exchanging residues 88-123 of secretory MMP-7 with the same region in MMP-26 causes localization of this MMP-7 construct to the ER
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mutant enzyme shows high rates of fluorescent synthetic peptide hydrolysis
D114A
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mutation induces enhanced affinity for the Ca2+ ion or an irreversible loss of enzymatic activity triggered by low-affinity calcium binding respectively
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calcium-independent high invasiveness is observed in the K189E mutant MDA-MB-231 cell line
K189E
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mutant enzyme shows high rates of fluorescent synthetic peptide hydrolysis
K189E
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mutation induces enhanced affinity for the Ca2+ ion or an irreversible loss of enzymatic activity triggered by low-affinity calcium binding respectively