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
ECTree
3.4.24.B7 matrix metalloproteinase-26Advanced search results
results (
results (Substrates Products
Substrates Products on EC 3.4.24.B7 - matrix metalloproteinase-26
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(7-methoxycoumarin)-4-yl-acetyl-Pro-Leu-Ala-Nva-(N-3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-Ala-Arg-NH2 + H2O
(7-methoxycoumarin)-4-yl-acetyl-Pro-Leu-Ala + Nva-(N-3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-Ala-Arg-NH2
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among the fluorescent peptide substrates analyzed, 7-amido-4-methylcoumaryl-Pro-Leu-Ala-Nva-(N-3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-Ala-Arg-NH2 displays the highest specificity constant
-
-
?
(7-methoxycoumarin)-4-yl-acetyl-Pro-Leu-Gly-Leu-(N-3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-Ala-Arg-NH2 + H2O
?
-
-
-
-
?
(7-methoxycoumarin-4-yl)acetyl-PLAQAV-Dpa-RSSSR-NH2 + H2O
?
synthetic fluorogenic peptide derived of tumor necrosis factor-alpha converting enzyme
-
?
(7-methoxycoumarin-4-yl)acetyl-Pro-Cha-Gly-norvaline-His-Ala-Dpa-NH2 + H2O
?
synthetic fluorogenic substrate
-
?
(7-methoxycoumarin-4-yl)acetyl-RPKPVA-norvaline-WMK-(2,4-dinitrophenyl)-NH2 + H2O
?
synthetic fluorogenic peptide, catalytic domain of the enzyme
-
?
(7-methoxycoumarin-4-yl)acetyl-RPKPVE-norvaline-WMK-(2,4-dinitrophenyl)-NH2 + H2O
?
synthetic fluorogenic peptide derived of matrix metalloproteinases
-
?
insulin-like growth factor-binding protein-1 + H2O
?
-
cleaves His140Val141 in insulin-like growth factor-binding protein-1, probably rendering the substrate inactive
-
-
?
peptide + H2O
?
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the optimal cleavage motifs for MMP-26 are Lys-Pro-Ile(Leu)-Ser-/-Leu(Met)-Ile(Thr)-Ser(Ala)-Ser. The strongest preference is observed at the P1' and P2 sites where hydrophobic residues are favored. Proline is preferred at P3, and serine is preferred at P1
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-
?
progelatinase B + H2O
gelatinase B
substrate becomes activated, both enzymes can act as coordinately as part of a proteolytic cascade
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?
(7-methoxycoumarin-4-yl)acetyl-PKPLAL-Dpa-AR-NH2 + H2O
?
synthetic fluorogenic peptide derived of matrix metalloproteinases
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?
(7-methoxycoumarin-4-yl)acetyl-PKPLAL-Dpa-AR-NH2 + H2O
?
synthetic fluorogenic peptide, catalytic domain of the enzyme
-
?
(7-methoxycoumarin-4-yl)acetyl-PLGL-Dpa-AR-NH2 + H2O
?
synthetic fluorogenic substrate
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?
(7-methoxycoumarin-4-yl)acetyl-PLGL-Dpa-AR-NH2 + H2O
?
-
synthetic fluorogenic peptide
-
?
(7-methoxycoumarin-4-yl)acetyl-PLGL-Dpa-AR-NH2 + H2O
?
synthetic fluorogenic peptide derived of matrix metalloproteinases
-
?
(7-methoxycoumarin-4-yl)acetyl-PLGL-Dpa-AR-NH2 + H2O
?
synthetic fluorogenic peptide, derived from the catalytic domain of the enzyme
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?
(7-methoxycoumarin-4-yl)acetyl-RPKPYA-norvaline-WMK-(2,4-dinitrophenyl)-NH2 + H2O
?
synthetic fluorogenic peptide derived of matrix metalloproteinases
-
?
(7-methoxycoumarin-4-yl)acetyl-RPKPYA-norvaline-WMK-(2,4-dinitrophenyl)-NH2 + H2O
?
synthetic fluorogenic peptide, catalytic domain of the enzyme
-
?
alpha1-antitrypsin + H2O
?
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MMP-26 by cleaving and inactivating the alpha1-antitrypsin serpin, operates as a unique functional link that regulates a coordinated interplay between Ser and metalloproteinases in estrogen-dependent neoplasm. Involvement of MMP-26 in inflammation and malignant progression of estrogen-dependent tumor
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-
?
alpha1-antitrypsin + H2O
?
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the enzyme is highly efficient in cleaving the the serpin alpha1-antitrypsin at the positions Gln135-/-Leu136, Glu223-/-Val224, Phe376-/-Leu377, and Pro381-/-Met382
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-
?
alpha1-proteinase inhibitor + H2O
?
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MMP-26 cleaves Phe352Leu353 and Pro357Met358 in the reactive loop of alpha1-proteinase inhibitor, probably rendering the substrate inactive
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-
?
Fibrinogen + H2O
?
complete degradation, cleavage sequenced of the peptide chains, overview
-
?
pro-MMP-9 + H2O
MMP-9 + MMP-9 propeptide
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MMP-26 can activate MMP-9 by cleavage of some sites in pro-MMP-9
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-
?
proteins + H2O
peptides
enzyme might be rsponsible for inactivation of cytokins and serpins
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?
proteins + H2O
peptides
enzyme plays an important specific role in tumor progression and angiogenesis
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?
proteins + H2O
peptides
potentially implicated in tumor progression
-
?
Vitronectin + H2O
?
complete degradation, cleavage sequence is PPEG134-I135DSR
-
?
additional information
?
-
no activity with collagens, laminin, elastin, beta-casein, plasminogen, soybean trypsin inhibitor, Bowman-Birk inhibitor
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?
additional information
?
-
-
no activity with collagens, laminin, elastin, beta-casein, plasminogen, soybean trypsin inhibitor, Bowman-Birk inhibitor
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?
additional information
?
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increased level and activation of MMP-26 in gingival crevicular fluid is associated with an enhanced severity of periodontal inflammation, suggesting that MMP-26 can participate in the progression of periodontal diseases
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-
?
additional information
?
-
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the enzyme exhibits an unconventional PH81CGVPD Cys switch motif
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-
?
