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

for references in articles please use BRENDA:EC3.4.24.B5
preliminary BRENDA-supplied EC number
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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.24 Metalloendopeptidases
                3.4.24.B5 matrix metalloproteinase-15
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Homo sapiens
UNIPROT: P50281
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
proteolytic degradation of proteins
Synonyms
mt2-mmp, mmp15, mmp-15, membrane-type matrix metalloproteinase, membrane-type-1 matrix metalloproteinase, matrix metalloproteinase 15, mt1 mmp, matrix metalloproteinase-15, membrane-type-2 matrix metalloproteinase, membrane type 2-mmp, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
M10.015
Merops-ID
membrane-type matrix metalloproteinase
-
membrane-type-1 matrix metalloproteinase
-
membrane-type-2 matrix metalloproteinase
-
membrane-type-3 matrix metalloproteinase
-
M10.015
matrix metalloproteinase 15
membrane type 2 matrix metalloproteinase
-
-
membrane-type matrix metalloproteinase 2
-
membrane-type-1 matrix metalloproteinase
-
-
membrane-type-2 matrix metalloproteinase
membrane-type-3 matrix metalloproteinase
-
-
MMP-15
MMP15
MT1 MMP
-
-
MT2 MMP
-
-
MT2-MMP
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
hydrolysis of peptide bond
CAS REGISTRY NUMBER
COMMENTARY hide
172308-17-7
-
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 of cell surface tissue transglutaminase
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
-
?
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
-
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
-
weak collagenase activity
-
-
?
additional information
?
-
the enzyme does not cleave endoglin
-
-
?
NATURAL SUBSTRATE
NATURAL 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
?
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
-
?
protein + H2O
peptides
show the reaction diagram
-
-
?
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
?
-
the enzyme does not cleave endoglin
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
fibronectin
protects the cell surface tissue transglutaminase against degradation by MT1 MMP
-
matrix metalloproteinase inhibitor TIMP-2
-
regulatory function, forms complex with the enzyme on the surface of cells
-
TIMP-2
-
inhibitory above 10 nM
-
tissue matrix metalloproteinase inhibitor TIMP-2
-
-
-
tissue matrix metalloproteinase inhibitor TIMP-3
-
-
-
additional information
-
no inhibition by tissue matrix metalloproteinase inhibitor TIMP-1
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
12-O-tetradecanoyl phorbol 13-acetate
-
activates enzyme expression
Collagen
-
enhances MMP-2 activation by MT2-MMP
concanavalin A
-
regulatory role, activates enzyme expression and activity, effect is inhibited by matrix metalloproteinase inhibitor TIMP-2
-
tissue matrix metalloprotease inhibitor TIMP-2
-
regulatory role, expression and protein levels in cancer cell lines are not corresponding, overview
-
additional information
-
TIMPs 1-4 and claudin-5 do not enhance MMP-2 activation by MT2-MMP
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
assay at
7.5
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
assay at
37
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
membrane-type-1, -type -2 and -type-3 matrix metalloproteases
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
low expression level
Manually annotated by BRENDA team
low expression level
Manually annotated by BRENDA team
-
high expression of MMP-15 in tumour samples
Manually annotated by BRENDA team
peripheral
Manually annotated by BRENDA team
-
cancer cell line, low expression of MT2 MMP
Manually annotated by BRENDA team
-
squamous carcinoma cell line, expresssion of MT2 MMP not MT1 MMP and MT3 MMP
Manually annotated by BRENDA team
-
squamous carcinoma cell line, expresssion of MT2 MMP not MT1 MMP and MT3 MMP
Manually annotated by BRENDA team
-
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
overexpression of MMP-15 in human lung adenocarcinoma compared with normal lung
Manually annotated by BRENDA team
has lowest MMP-15 expression of all cell lines
Manually annotated by BRENDA team
MMP15 is overexpressed in acute myeloid leukemia (AML) patients
Manually annotated by BRENDA team
-
MMP-15 expression is significantly lower in tumor tissue compared with normal tissue
Manually annotated by BRENDA team
-
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
-
cancer cell line, low expression of MT2 MMP
Manually annotated by BRENDA team
-
cancer cell line, low expression of MT2 MMP
Manually annotated by BRENDA team
primary human trophoblasts from 50 first trimester placentas (gestational week 7-12), high MMP115 expression
Manually annotated by BRENDA team
-
cancer cell line, low expression of MT2 MMP and expression of MT3 MMP
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
on the cell surface
Manually annotated by BRENDA team
-
on the cell surface
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
MMP14 and MMP15 are involved in trophoblast invasion
physiological function
enzyme MMP15 mainly play roles in extracellular matrix disassembly
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
MMP14_HUMAN
582
1
65894
Swiss-Prot
-
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
-
recombinant form of the MT2-MMP hemopexin C domain with linker
66000
-
fully active enzyme, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 42000, MT1 MMP ectodomain, SDS-PAGE, x * 60000, MT1 MMP, active enzyme, SDS-PAGE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni2+-chelate column chromatography, CM-Sepharose column chromatography, and Q Sepharose column cromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
functional expression of enzyme in HT1080 cells and U251 glioma cells, leading to enhanced levels of pro-matrix metalloprotease-2
cloned into pcDNA 3.1/myc-His and subcloned into pLXSN to yield myc-His-tagged MMP-15
expressed in Escherichia coli and in Timp2-/- skin fibroblasts
-
expression of the enzymes catalytic domain in Escherichia coli
-
gene MMP15, quantitative expression analysis
gene MMP15, quantitative RT-PCR enzyme expression analysis
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
endothelin-1 (ET-1) downregulates matrix metalloproteinase 15 expression in human first trimester trophoblasts via endothelin receptor type B (ETRB). ET-1 downregulates MMP15 mRNA and protein levels. TNF-alpha enhances ET-1-mediated MMP15 downregulation in primary trophoblasts
the enzyme is significantly up-regulated in placentas from severe early-onset preeclamptic pregnancies compared to gestationally matched preterm controls
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
diagnostics
potential role of MMP15 in the prognosis of acute myeloid leukemia (AML). MMP7 and MMP15 expression is associated with various clinicopathological characteristics in AML, but MMP7 or MMP15 expression signature are not independent prognostic factors in AML as compared with risk stratifications
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Boeckmann, B.; Bairoch, A.; Apweiler, R.; Blatter, M.C.; Estreicher, A.; Gasteiger, E.; Martin M.J.; Michoud, K.; O'Donovan, C.; Phan, I.; Pilbout, S.; Schneider, M.
The SWISS-PROT protein knowledgebase and its supplement TrEMBL
Nucleic Acids Res.
31
365-370
2003
Homo sapiens (P51511), Mus musculus (O54732)
Manually annotated by BRENDA team
Butler, G.S.; Will, H.; Atkinson, S.J.; Murphy, G.
Membrane-type-2 matrix metalloproteinase can initiate the processing of progelatinase A and is regulated by the tissue inhibitors of metalloproteinases
Eur. J. Biochem.
244
653-657
1997
Homo sapiens
Manually annotated by BRENDA team
Shofuda, K.I.; Moriyama, K.; Nishihashi, A.; Higashi, S.; Mizushima, H.; Yasumitsu, H.; Miki, K.; Sato, H.; Seiki, M.; Miyazaki, K.
Role of tissue inhibitor of metalloproteinases-2 (TIMP-2) in regulation of pro-gelatinase A activation catalyzed by membrane-type matrix metalloproteinase-1 (MT1-MMP) in human cancer cells
J. Biochem.
124
462-470
1998
Homo sapiens
Manually annotated by BRENDA team
Belkin, A.M.; Akimov, S.S.; Zaritskaya, L.S.; Ratnikov, B.I.; Deryugina, E.I.; Strongin, A.Y.
Matrix-dependent proteolysis of surface transglutaminase by membrane-type metalloproteinase regulates cancer cell adhesion and locomotion
J. Biol. Chem.
276
18415-18422
2001
Homo sapiens (P50281)
Manually annotated by BRENDA team
Wallard, M.J.; Pennington, C.J.; Veerakumarasivam, A.; Burtt, G.; Mills, I.G.; Warren, A.; Leung, H.Y.; Murphy, G.; Edwards, D.R.; Neal, D.E.; Kelly, J.D.
Comprehensive profiling and localisation of the matrix metalloproteinases in urothelial carcinoma
Br. J. Cancer
94
569-577
2006
Homo sapiens
Manually annotated by BRENDA team
Jones, L.E.; Humphreys, M.J.; Campbell, F.; Neoptolemos, J.P.; Boyd, M.T.
Comprehensive analysis of matrix metalloproteinase and tissue inhibitor expression in pancreatic cancer: increased expression of matrix metalloproteinase-7 predicts poor survival
Clin. Cancer Res.
10
2832-2845
2004
Homo sapiens
Manually annotated by BRENDA team
Abraham, R.; Schaefer, J.; Rothe, M.; Bange, J.; Knyazev, P.; Ullrich, A.
Identification of MMP-15 as an anti-apoptotic factor in cancer cells
J. Biol. Chem.
280
34123-34132
2005
Homo sapiens (P51511), Homo sapiens
Manually annotated by BRENDA team
Hiden, U.; Wadsack, C.; Prutsch, N.; Gauster, M.; Weiss, U.; Frank, H.G.; Schmitz, U.; Fast-Hirsch, C.; Hengstschlaeger, M.; Poetgens, A.; Rueben, A.; Knoefler, M.; Haslinger, P.; Huppertz, B.; Bilban, M.; Kaufmann, P.; Desoye, G.
The first trimester human trophoblast cell line ACH-3P: a novel tool to study autocrine/paracrine regulatory loops of human trophoblast subpopulations - TNF-alpha stimulates MMP15 expression
BMC Dev. Biol.
7
137
2007
Homo sapiens
Manually annotated by BRENDA team
Morrison, C.J.; Overall, C.M.
TIMP independence of matrix metalloproteinase (MMP)-2 activation by membrane type 2 (MT2)-MMP is determined by contributions of both the MT2-MMP catalytic and hemopexin C domains
J. Biol. Chem.
281
26528-26539
2006
Homo sapiens
Manually annotated by BRENDA team
Kaituu-Lino, T.J.; Palmer, K.; Tuohey, L.; Ye, L.; Tong, S.
MMP-15 is upregulated in preeclampsia, but does not cleave endoglin to produce soluble endoglin
PLoS ONE
7
e39864
2012
Homo sapiens (P51511)
Manually annotated by BRENDA team
Majali-Martinez, A.; Velicky, P.; Pollheimer, J.; Knoefler, M.; Yung, H.W.; Burton, G.J.; Tabrizi-Wizsy, N.G.; Lang, U.; Hiden, U.; Desoye, G.; Dieber-Rotheneder, M.
Endothelin-1 down-regulates matrix metalloproteinase 14 and 15 expression in human first trimester trophoblasts via endothelin receptor type B
Hum. Reprod.
32
46-54
2017
Homo sapiens (P51511), Homo sapiens
Manually annotated by BRENDA team
Wu, Y.; Pan, S.; Leng, J.; Xie, T.; Jamal, M.; Yin, Q.; Li, J.; He, C.; Dong, X.; Shao, L.; Zhang, Q.
The prognostic value of matrix metalloproteinase-7 and matrix metalloproteinase-15 in acute myeloid leukemia
J. Cell. Biochem.
120
10613-10624
2019
Homo sapiens (P51511), Homo sapiens
Manually annotated by BRENDA team