Information on EC 3.4.24.B5 - matrix metalloproteinase-15 and Organism(s) Homo sapiens and UniProt Accession P50281

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Homo sapiens
UNIPROT: P50281


The taxonomic range for the selected organisms is: Homo sapiens

The enzyme appears in selected 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 TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
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hydrolysis of peptide bond
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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-
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CAS REGISTRY NUMBER
COMMENTARY hide
172308-17-7
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
membrane-type-1, -type -2 and -type-3 matrix metalloproteases
SwissProt
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
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
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
-
?
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
-
?
progelatinase A + H2O
gelatinase A
show the reaction diagram
substrate is activated by cleavage
-
?
protein + H2O
peptides
show the reaction diagram
(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
-
synthetic fluorogenic substrate
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?
matrix metalloproteinase progelatinase A + H2O
matrix metalloproteinase gelatinase A
show the reaction diagram
-
substrate is activated by cleavage
-
?
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
-
-
?
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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-
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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
-
?
protein + H2O
peptides
show the reaction diagram
P50281
-
-
?
matrix metalloproteinase progelatinase A + H2O
matrix metalloproteinase gelatinase A
show the reaction diagram
-
substrate is activated by cleavage
-
?
protein + H2O
peptides
show the reaction diagram
additional information
?
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the enzyme does not cleave endoglin
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-
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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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-
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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
7.5
assay at
7.5
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assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
assay at
37
-
assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
low expression level
Manually annotated by BRENDA team
low expression level
Manually annotated by BRENDA team
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high expression of MMP-15 in tumour 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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expresssion of MT2 MMP not MT1 MMP and MT3 MMP, cancer cell line, expressing the proform gelatinase A, concanavalin A supresses the expression of MT1 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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has lowest MMP-15 expression of all cell lines
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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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
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cancer cell line, low expression of MT2 MMP and expression of MT3 MMP
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
on the cell surface
Manually annotated by BRENDA team
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on the cell surface
Manually annotated by BRENDA team
PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
31400
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recombinant form of the MT2-MMP hemopexin C domain with linker
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