Information on EC 3.4.24.B5 - matrix metalloproteinase-15

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.4.24.B5
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
matrix metalloproteinase-15
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
proteolytic degradation of proteins
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
CAS REGISTRY NUMBER
COMMENTARY hide
172308-17-7
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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-Gly-Leu-[3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl]-Ala-Arg-NH2 + H2O
?
show the reaction diagram
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synthetic fluorogenic substrate
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?
cell surface tissue transglutaminase + H2O
4 major and several minor cleavage products
show the reaction diagram
at the leading edge of motile cancer cells, membrane-type-1, -type -2 and -type-3 matrix metalloproteases
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?
cell surface tissue transglutaminase + H2O
?
show the reaction diagram
regulation of cancer cell adhesion, degradation supresses specifically cell adhesion and migration on fibronectin, but stimulates migration of cells on collagen
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?
matrix metalloproteinase progelatinase A + H2O
matrix metalloproteinase gelatinase A
show the reaction diagram
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substrate is activated by cleavage
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?
pro-form of matrix metalloproteinase 2 + H2O
active form of matrix metalloproteinase 2
show the reaction diagram
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MMP-2 hemopexin carboxyl domain-dependent activation process
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-
?
progelatinase A + H2O
gelatinase A
show the reaction diagram
protein + H2O
peptides
show the reaction diagram
Type I collagen + H2O
?
show the reaction diagram
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weak collagenase activity
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?
additional information
?
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the enzyme does not cleave endoglin
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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
cell surface tissue transglutaminase + H2O
?
show the reaction diagram
P50281
regulation of cancer cell adhesion, degradation supresses specifically cell adhesion and migration on fibronectin, but stimulates migration of cells on collagen
-
?
matrix metalloproteinase progelatinase A + H2O
matrix metalloproteinase gelatinase A
show the reaction diagram
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substrate is activated by cleavage
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?
protein + H2O
peptides
show the reaction diagram
additional information
?
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the enzyme does not cleave endoglin
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
fibronectin
protects the cell surface tissue transglutaminase against degradation by MT1 MMP
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matrix metalloproteinase inhibitor TIMP-2
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regulatory function, forms complex with the enzyme on the surface of cells
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TIMP-2
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inhibitory above 10 nM
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tissue matrix metalloproteinase inhibitor TIMP-2
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tissue matrix metalloproteinase inhibitor TIMP-3
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additional information
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no inhibition by tissue matrix metalloproteinase inhibitor TIMP-1
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
12-O-tetradecanoyl phorbol 13-acetate
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activates enzyme expression
Collagen
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enhances MMP-2 activation by MT2-MMP
concanavalin A
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regulatory role, activates enzyme expression and activity, effect is inhibited by matrix metalloproteinase inhibitor TIMP-2
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tissue matrix metalloprotease inhibitor TIMP-2
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regulatory role, expression and protein levels in cancer cell lines are not corresponding, overview
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additional information
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TIMPs 1-4 and claudin-5 do not enhance MMP-2 activation by MT2-MMP
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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high expression of MMP-15 in tumour samples
Manually annotated by BRENDA team
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trends in expression of MMP-15 is similar between brain and spinal cord samples
Manually annotated by BRENDA team
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cancer cell line, low expression of MT2 MMP
Manually annotated by BRENDA team
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squamous carcinoma cell line, expresssion of MT2 MMP not MT1 MMP and MT3 MMP
Manually annotated by BRENDA team
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squamous carcinoma cell line, expresssion of MT2 MMP not MT1 MMP and MT3 MMP
Manually annotated by BRENDA team
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overexpression of MMP-15 in human lung adenocarcinoma compared with normal lung
Manually annotated by BRENDA team
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small expression
Manually annotated by BRENDA team
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MMP-15 is expressed at a significantly higher level by myeloid cells than by T cells
Manually annotated by BRENDA team
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has lowest MMP-15 expression of all cell lines
Manually annotated by BRENDA team
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MMP-15 is mainly expressed by resting microglia, and this is reduced 15fold in experimental autoimmune encephalomyelitis
Manually annotated by BRENDA team
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MMP-15 expression is significantly lower in tumor tissue compared with normal tissue
Manually annotated by BRENDA team
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MMP-15 message is down-regulated 5.5fold in experimental autoimmune encephalomyelitis
Manually annotated by BRENDA team
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in tumour tissues MMP-15 is expressed at a significantly higher level in stroma tissue when compared to tissue fromt the epithelially derived compartment
Manually annotated by BRENDA team
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cancer cell line, low expression of MT2 MMP
Manually annotated by BRENDA team
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cancer cell line, low expression of MT2 MMP
Manually annotated by BRENDA team
low expression level
Manually annotated by BRENDA team
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cancer cell line, low expression of MT2 MMP and expression of MT3 MMP
Manually annotated by BRENDA team
additional information
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T-cell
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
31400
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recombinant form of the MT2-MMP hemopexin C domain with linker
42000
x * 42000, MT1 MMP ectodomain, SDS-PAGE, x * 60000, MT1 MMP, active enzyme, SDS-PAGE
60000
x * 42000, MT1 MMP ectodomain, SDS-PAGE, x * 60000, MT1 MMP, active enzyme, SDS-PAGE
66000
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fully active enzyme, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 42000, MT1 MMP ectodomain, SDS-PAGE, x * 60000, MT1 MMP, active enzyme, SDS-PAGE
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Ni2+-chelate column chromatography, CM-Sepharose column chromatography, and Q Sepharose column cromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cloned into pcDNA 3.1/myc-His and subcloned into pLXSN to yield myc-His-tagged MMP-15
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expressed in Escherichia coli and in Timp2-/- skin fibroblasts
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expression of the enzymes catalytic domain in Escherichia coli
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functional expression of enzyme in HT1080 cells and U251 glioma cells, leading to enhanced levels of pro-matrix metalloprotease-2
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the enzyme is significantly up-regulated in placentas from severe early-onset preeclamptic pregnancies compared to gestationally matched preterm controls
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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knock-down of MMP-15 increases cell death rate
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine