Information on EC 3.4.24.B7 - matrix metalloproteinase-26

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.4.24.B7
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
matrix metalloproteinase-26
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
proteolytic degradation of proteins
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
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CAS REGISTRY NUMBER
COMMENTARY hide
288381-81-7
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
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silencing of the MMP-26 gene significantly retardes the invasiveness of A-549 cells
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
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
show the reaction diagram
-
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
?
show the reaction diagram
-
-
-
-
?
(7-methoxycoumarin-4-yl)acetyl-PKPLAL-Dpa-AR-NH2 + H2O
?
show the reaction diagram
(7-methoxycoumarin-4-yl)acetyl-PLAQAV-Dpa-RSSSR-NH2 + H2O
?
show the reaction diagram
-
synthetic fluorogenic peptide derived of tumor necrosis factor-alpha converting enzyme
-
?
(7-methoxycoumarin-4-yl)acetyl-PLGL-Dpa-AR-NH2 + H2O
?
show the reaction diagram
(7-methoxycoumarin-4-yl)acetyl-Pro-Cha-Gly-norvaline-His-Ala-Dpa-NH2 + H2O
?
show the reaction diagram
synthetic fluorogenic substrate
-
?
(7-methoxycoumarin-4-yl)acetyl-RPKPVA-norvaline-WMK-(2,4-dinitrophenyl)-NH2 + H2O
?
show the reaction diagram
synthetic fluorogenic peptide, catalytic domain of the enzyme
-
?
(7-methoxycoumarin-4-yl)acetyl-RPKPVE-norvaline-WMK-(2,4-dinitrophenyl)-NH2 + H2O
?
show the reaction diagram
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synthetic fluorogenic peptide derived of matrix metalloproteinases
-
?
(7-methoxycoumarin-4-yl)acetyl-RPKPYA-norvaline-WMK-(2,4-dinitrophenyl)-NH2 + H2O
?
show the reaction diagram
activated pro-MMP-9 + H2O
?
show the reaction diagram
-
-
-
-
?
alpha1-antitrypsin + H2O
?
show the reaction diagram
alpha1-proteinase inhibitor + H2O
?
show the reaction diagram
casein + H2O
?
show the reaction diagram
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zymography
-
-
?
denatured collagen + H2O
?
show the reaction diagram
-
-
?
denatured collagen type I + H2O
?
show the reaction diagram
-
-
-
-
?
denatured collagen type II + H2O
?
show the reaction diagram
-
-
-
-
?
denatured collagen type III + H2O
?
show the reaction diagram
-
-
-
-
?
denatured collagen type IV + H2O
?
show the reaction diagram
-
-
-
-
?
DQ-gelatin + H2O
?
show the reaction diagram
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fluorescein conjugated substrate from pig skin
-
-
?
Fibrinogen + H2O
?
show the reaction diagram
Fibronectin + H2O
?
show the reaction diagram
Gelatin + H2O
?
show the reaction diagram
insulin-like growth factor binding protein 1 + H2O
?
show the reaction diagram
-
-
-
-
?
insulin-like growth factor-binding protein-1 + H2O
?
show the reaction diagram
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cleaves His140Val141 in insulin-like growth factor-binding protein-1, probably rendering the substrate inactive
-
-
?
peptide + H2O
?
show the reaction diagram
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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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-
?
pro-MMP-9 + H2O
MMP-9 + MMP-9 propeptide
show the reaction diagram
progelatinase B + H2O
gelatinase B
show the reaction diagram
substrate becomes activated, both enzymes can act as coordinately as part of a proteolytic cascade
-
?
proteins + H2O
peptides
show the reaction diagram
type I gelatin + H2O
?
show the reaction diagram
-
-
-
?
Type IV collagen + H2O
?
show the reaction diagram
vibronectin + H2O
?
show the reaction diagram
-
-
-
-
?
Vitronectin + H2O
?
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
activated pro-MMP-9 + H2O
?
show the reaction diagram
-
-
-
-
?
alpha1-antitrypsin + H2O
?
show the reaction diagram
-
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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-
?
denatured collagen type I + H2O
?
show the reaction diagram
-
-
-
-
?
denatured collagen type II + H2O
?
show the reaction diagram
-
-
-
-
?
denatured collagen type III + H2O
?
show the reaction diagram
-
-
-
-
?
denatured collagen type IV + H2O
?
show the reaction diagram
-
-
-
-
?
Fibrinogen + H2O
?
show the reaction diagram
-
-
-
-
?
Fibronectin + H2O
?
show the reaction diagram
-
-
-
-
?
Gelatin + H2O
?
show the reaction diagram
-
-
-
-
?
insulin-like growth factor binding protein 1 + H2O
?
show the reaction diagram
-
-
-
-
?
pro-MMP-9 + H2O
MMP-9 + MMP-9 propeptide
show the reaction diagram
proteins + H2O
peptides
show the reaction diagram
Type IV collagen + H2O
?
show the reaction diagram
-
-
-
-
?
vibronectin + H2O
?
show the reaction diagram
-
-
-
-
?
Vitronectin + H2O
?
show the reaction diagram
-
-
-
-
?
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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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
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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4-Aminobenzoyl-Gly-Pro-D-Leu-D-Ala-NHOH
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AG3340
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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
hydroxamate inhibitors
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hydroxamate matrix metalloproteinase inhibitors
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MAG-181
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; mercaptosulfide matrix metalloproteinase inhibitor
MAG-182
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; mercaptosulfide matrix metalloproteinase inhibitor
matrix metalloproteinase inhibitor BB-94
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matrix metalloproteinase inhibitor GM6001
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matrix metalloproteinase inhibitor TIMP-1
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matrix metalloproteinase inhibitor TIMP-2
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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
YHJ-294-1
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; mercaptosulfide matrix metalloproteinase inhibitor
YHJ-294-2
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; mercaptosulfide matrix metalloproteinase inhibitor
YHJ-72
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; mercaptosulfide matrix metalloproteinase inhibitor
YHJ-73
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; mercaptosulfide matrix metalloproteinase inhibitor
YHJ-74
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; mercaptosulfide matrix metalloproteinase inhibitor
YHJ-75
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; mercaptosulfide matrix metalloproteinase inhibitor
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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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
SDS
-
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
-
optimally activating at 0.140 mM, at concentrations above the critical micelle concentration
Tween 20
-
optimally activating at 0.079 mM, at concentrations above the critical micelle concentration
additional information
-
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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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0000015
(3R)-N-hydroxy-2-[(4-methoxyphenyl)sulfonyl]-1,2,3,4-tetrahydroisoquinoline-3-carboxamide
-
-
0.00006
(3S)-N-hydroxy-2-[(4-methoxyphenyl)sulfonyl]-1,2,3,4-tetrahydroisoquinoline-3-carboxamide
-
-
0.0000029
4-Aminobenzoyl-Gly-Pro-D-Leu-D-Ala-NHOH
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-
0.0000015
AG3340
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-
0.24
Brij-35
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pH 7.5, 25C
0.000081
MAG-181
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pH 7.5, 25C
0.000017
MAG-182
-
pH 7.5, 25C
0.00000036
N-[(2R)-2-(hydroxamidocarbonylmethyl)-4-methylpentanoyl]-L-tryptophan
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-
0.00045
YHJ-294-1
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pH 7.5, 25C
0.0000028
YHJ-294-2
-
pH 7.5, 25C
0.00016
YHJ-72
-
pH 7.5, 25C
0.000028
YHJ-73
-
pH 7.5, 25C
0.000082
YHJ-74
-
pH 7.5, 25C
0.0000086
YHJ-75
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pH 7.5, 25C
additional information
additional information
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0034
4-Aminobenzoyl-Gly-Pro-D-Leu-D-Ala-NHOH
Homo sapiens
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-
0.56
Brij-35
Homo sapiens
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pH 7.5, 25C
0.11
SDS
Homo sapiens
-
pH 7.5, 25C
0.079
Tetradecyltrimethylammonium bromide
Homo sapiens
-
pH 7.5, 25C
1.3
Triton X-100
Homo sapiens
-
pH 7.5, 25C
0.64
Tween 20
Homo sapiens
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pH 7.5, 25C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
133000000
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fluorescent units/mg, pH 7.5, 22C
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.8
-
assay at
7.4
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assay at
7.5
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assay at
7.6
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
-
assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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epithelium and stroma of adenomatoid odontogenic tumors, overview
Manually annotated by BRENDA team
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epithelium and stroma of amelobastomas, overview
Manually annotated by BRENDA team
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an immortalized cytotrophoblast-like cell line
Manually annotated by BRENDA team
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elevated MMP-26 expression level
Manually annotated by BRENDA team
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elevated MMP-26 expression level
Manually annotated by BRENDA team
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decending and transverse, gene expression
Manually annotated by BRENDA team
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beta-catenin regulates the gene of MMP-26, a novel metalloproteinase expressed both in carcinomas and normal epithelial cells
Manually annotated by BRENDA team
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elevated MMP-26 expression level
Manually annotated by BRENDA team
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primary cell culture
Manually annotated by BRENDA team
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apical epithelial conjunctiva cells of the human eye
Manually annotated by BRENDA team
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slightly enhanced MMP-26 staining in HIV+ gingival tissue samples in comparison with controls
Manually annotated by BRENDA team
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from patients with aggressive periodontitis, with chronic periodontitis, with gingivitis and periodontally healthy subjects. Patients with aggressive periodontitis and patients with chronic periodontitis have elevated MMP-26 levels and degrees of activation compared with the gingivitis and healthy groups. The gingivitis group has higher MMP-26 levels and degree of activation compared to the healthy group
Manually annotated by BRENDA team
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in intact skin MMP-26 is expressed only in hair follicles
Manually annotated by BRENDA team
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-
Manually annotated by BRENDA team
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elevated MMP-26 expression level
Manually annotated by BRENDA team
promyelocytic leukemia, gene expression
Manually annotated by BRENDA team
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constitutive expression. Protein is found in both disc cells and in the disc extracellular matrix. MMP-26 is identified in the outer and inner annulus and in the nucleus pulposus. Fewer cells show localization in the inner vs. outer annulus, and localization is sparse in the nucleus; in the outer and inner annulus and in the nucleus pulposus
Manually annotated by BRENDA team
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a choriocarcinoma cell line
Manually annotated by BRENDA team
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matrilysin-2 (matrix metalloproteinase-26) is upregulated in keratinocytes during wound repair and early skin carcinogenesis. MMP-26 is expressed by laminin-5-positive keratinocytes in the migrating area during wound repair, in benign skin disorders characterized by inflammation and microdisruptions of basement membrane. MMP-26 may be upregulated in basal keratinocytes even without tumorigenesis because of altered cell-matrix interactions and inflammation
Manually annotated by BRENDA team
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of peripheral blood, gene expression
Manually annotated by BRENDA team
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-
Manually annotated by BRENDA team
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in the course of further disease progression through stages I to III, the expression of MMP-26 decreases. The expression of MMP-26 in ductal carcinomas correlates with a longer patient survival
Manually annotated by BRENDA team
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elevated MMP-26 expression level
Manually annotated by BRENDA team
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-
Manually annotated by BRENDA team
-
no elevated MMP-26 expression level
Manually annotated by BRENDA team
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high expression rate of MMP-26
Manually annotated by BRENDA team
-
no elevated MMP-26 expression level
Manually annotated by BRENDA team
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patients with metastatic lymph nodeshave increased expression of MMP-26 in tumor samples
Manually annotated by BRENDA team
gene expression
Manually annotated by BRENDA team
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from control and preeclamptic umbilical cord blood
Manually annotated by BRENDA team
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matrix metalloproteinase-26 is associated with macrophages and polymorphonuclear leukocytes
Manually annotated by BRENDA team
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from control and preeclamptic umbilical cord blood
Manually annotated by BRENDA team
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fetal, gene expression
Manually annotated by BRENDA team
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gene expression
Manually annotated by BRENDA team
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from coronary artery or from prostate tissue and associated blood vessels
Manually annotated by BRENDA team
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gene expression
Manually annotated by BRENDA team
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chondrosarcoma cell line
Manually annotated by BRENDA team
colorectal adenocarcinoma, gene expression
Manually annotated by BRENDA team
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gene expression
Manually annotated by BRENDA team
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fetal, gene expression
Manually annotated by BRENDA team
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MMP-26 mRNA is evenly distributed in all glandular epithelial cells and luminal epithelial cells but is absent in the stroma. The amount of MMP-26 mRNA is greater in samples at day 5 in an artificial cycle of progesterone addition than at day 7 in an artificial cycle of progesterone addition
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
19000
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x * 19000, SDS-PAGE of catalytic form, x * 28000, SDS-PAGE of His-tagged proform
29000
-
proenzyme, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
2 N-glycosylation sites at residues 64 and 133
proteolytic modification
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
high-affinity calcium binding protects MMP-26 against thermal denaturation
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant catalytic domain from inclusion bodies expressed in Escherichia coli
-
recombinant from Escherichia coli, to homogeneity
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recombinant His-tagged protein from Escherichia coli
recombinant protein
-
recombinantly expressed proenzyme
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, chromosomal mapping to the short arm of chromosome 11 around 11p15, expression in Escherichia coli as His-tagged protein
DNA and amino acid sequence determination and analysis, chromosome mapping to 11p15.3, expression of the enzymes catalytic domain in Escherichia coli BL21 (DE3)
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DNA sequence determination and analysis, expression of the zymogen in Escherichia coli
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expression in Brevibacillus choshinensis
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expression in Escherichia coli. Human breast cancer cell line, MDA-MB-231, transfected with wild-type MMP-26 cDNA shows a calcium-dependent invasive potential when compared with controls that were transfected with an inactive form of MMP-26 (E209A)
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expression of proenzyme MMP-26 in Escherichia coli
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expression of proMMP-26 in Escherichia coli in inclusion bodies
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MMP-26 real-time PCR expression analysis
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transfection of MCF-7 cells
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U251 cells wae transfected with a proMMP-26 cDNA encoding vector, establishment of an MMP-26 overexpressing U251 cell model, overview
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
endometrial MMP26 expression is dependent on the presence of progesterone in the early secretory phase and then gradually becomes refractory to progesterone stimulation in the late secretory phase
regulatory effects of gonadotropin-releasing hormone I and gonadotropin-releasing hormone II, GnRH I and GnRH II, on the expression of MMP-26 in human immortalized cytotrophoblast-like cell line, B6Tert-1. The activation of JNK, but not ERK1/2, is required for GnRH I and II-stimulated MMP-26 production in B6Tert-1 cells and primary cytotrophoblasts
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significant downregulation of expression of MMP-26, and significant 9.8fold upregulation of TGF-beta in more degenerated discs versus healthier discs; there is significant downregulation of expression of MMP-26 in more degenerated discs vs. healthier discs
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D114A
-
mutant enzyme shows high rates of fluorescent synthetic peptide hydrolysis; mutation induces enhanced affinity for the Ca2+ ion or an irreversible loss of enzymatic activity triggered by low-affinity calcium binding respectively
D165A
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very low rates of hydrolysis that are less than 5% of that seen for wild-type MMP-26
E191A
-
very low rates of hydrolysis that are less than 5% of that seen for wild-type MMP-26
E209A
-
inactive mutant enzyme
H81R
-
mutation restores the conventional cysteine-switch in the prodomain but fails to induce the cysteine-swich activation
K189E
-
calcium-independent high invasiveness is observed in the K189E mutant MDA-MB-231 cell line; mutant enzyme shows high rates of fluorescent synthetic peptide hydrolysis; mutation induces enhanced affinity for the Ca2+ ion or an irreversible loss of enzymatic activity triggered by low-affinity calcium binding respectively
V184D
-
mutant enzyme shows high rates of fluorescent synthetic peptide hydrolysis
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant zymogen from inclusion bodies expressed in Escherichia coli, partial activation of th proform during refolding
-
refolding of recombinant catalytic domain from inclusion bodies expressed in Escherichia coli
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refolding of recombinant protein from inclusion bodies expressed in Escherichia coli
solubilization of recombinant proMMP-26 from Escherichia coli inclusion bodies by 8 M urea, followed by dialysis against 4 M urea, 1 mM DTT, and 50 mM HEPES or Tricine at pH 7.5 for at least 1 h, and then folded by dialysis against buffer containing 50 mM Hepes, 0.2 M, NaCl, 10 mM CaCl2, 20 lM ZnSO4, and 0.05% Brij-35 at pH 7.5 for 12 h three times, MMP-26 autoactivates
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
diagnostics
-
MMP-26 is a putative early biomarker for human carcinomas
medicine
synthesis
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use of Brevibacillus choshinensis as the host system for the soluble and active expression of MMP26. The enzyme is secreted in soluble form in the supernatant of cell culture medium. The yields of purified proform of MMP26 and catalytic form of MMP-26 are 12 and 18 mg/L, respectively, with high purity and homogeneity. Both pro- and catalytic form show gelatin zymography activity and the purified catalytic form has high enzymatic activity against DQ-gelatin substrate. Expression using several widely used expression vectors in Escheriochia coli cells results in insoluble expressions or soluble expressions with little catalytic activity