Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 3.4.24.B3 - matrix metalloproteinase-11 and Organism(s) Homo sapiens and UniProt Accession P24347

for references in articles please use BRENDA:EC3.4.24.B3
preliminary BRENDA-supplied EC number
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.24 Metalloendopeptidases
                3.4.24.B3 matrix metalloproteinase-11
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Homo sapiens
UNIPROT: P24347
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
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
mmp-11, mmp11, stromelysin-3, mp-11, stromelysin 3, matrix metalloproteinase 11, matrix metalloproteinase-11, mmp-11 proteinase, mmp stromelysin-3, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
M10.007
Merops-ID
matrix metalloproteinase-11
-
M10.007
-
Merops-ID
matrix metalloproteinase 11
-
-
matrix metalloproteinase-11
-
-
matrix metalloproteinase-11/stromelysin-3
-
-
matrixin
-
-
matrixin 11
-
-
MMP-11 proteinase
-
-
stromelysin 3
-
-
stromelysin-3
-
-
additional information
-
the enzyme belongs to the matrix metalloproteinase superfamily of Zn2+-dependent proteases
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
proteolytic degradation of proteins
show the reaction diagram
reaction and inhibition mechanism
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
hydrolysis of peptide bond
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
145267-01-2
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
protein + H2O
peptides
show the reaction diagram
-
-
?
alpha1-antitrypsin inhibitor + H2O
?
show the reaction diagram
-
-
-
?
alpha1-protease inhibitor + H2O
?
show the reaction diagram
-
-
-
?
casein + H2O
?
show the reaction diagram
-
only recombinant processed enzyme mutant A235P lacking the N-terminal prodomain and 175 amino acid residues of the C-terminus
-
?
collagen type IV + H2O
?
show the reaction diagram
-
only recombinant processed enzyme mutant A235P lacking the N-terminal prodomain and 175 amino acid residues of the C-terminus
-
?
collagen VI + H2O
?
show the reaction diagram
-
MMP11 cleaves the native alpha3 chain of collagen VI, which is an adipocyte-related extracellular matrix component. Extracellular proteolytic processing of this chain is required for correct collagen VI folding. MMP11-deficient fat tissue is less cohesive and exhibits collagen VI alteration, dramatic adipocyte plasma and basement membrane abnormalities and lipid leakage. MMP11 is thus required for correct collagen VI folding and therefore for fat tissue cohesion and adipocyte function. The native alpha3 chain of collagen VI constitutes a specific MMP11 substrate. This MMP11 collagenolytic activity is functional in fat tissue ontogenesis as well as during cancer invasive steps
-
-
?
dansyl-Pro-Leu-Ala-Met-Trp-Ala-Arg-NH2 + H2O
?
show the reaction diagram
-
-
-
-
?
GAAGAMFLEA + H2O
GAAGA + MFLEA
show the reaction diagram
-
-
-
?
GGAANLVRGG + H2O
GGAAN + LVRGG
show the reaction diagram
-
-
-
?
GGPLALWARGG + H2O
GGPLA + LWARGG
show the reaction diagram
-
-
-
?
GGPLGLYAGG + H2O
GGPLG + LYAGG
show the reaction diagram
-
-
-
?
GGQPRGVWGG + H2O
GGQPRG + VWGG
show the reaction diagram
-
-
-
?
GGTDAWLSGG + H2O
GGTDA + WLSGG
show the reaction diagram
-
-
-
?
GGYAELRMGG + H2O
GGYAE + LRMGG
show the reaction diagram
-
best substrate
-
?
insulin-like growth factor-binding protein-1 + H2O
2 peptides of 16 and 9 kDa MW
show the reaction diagram
-
specific for, cleavage site is the His140-Val141 bond
-
?
Laminin + H2O
?
show the reaction diagram
-
only recombinant processed enzyme mutant A235P lacking the N-terminal prodomain and 175 amino acid residues of the C-terminus
-
?
laminin receptor precursor + H2O
?
show the reaction diagram
-
-
-
-
?
protein + H2O
peptides
show the reaction diagram
additional information
?
-
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
protein + H2O
peptides
show the reaction diagram
-
-
?
collagen VI + H2O
?
show the reaction diagram
-
MMP11 cleaves the native alpha3 chain of collagen VI, which is an adipocyte-related extracellular matrix component. Extracellular proteolytic processing of this chain is required for correct collagen VI folding. MMP11-deficient fat tissue is less cohesive and exhibits collagen VI alteration, dramatic adipocyte plasma and basement membrane abnormalities and lipid leakage. MMP11 is thus required for correct collagen VI folding and therefore for fat tissue cohesion and adipocyte function. The native alpha3 chain of collagen VI constitutes a specific MMP11 substrate. This MMP11 collagenolytic activity is functional in fat tissue ontogenesis as well as during cancer invasive steps
-
-
?
protein + H2O
peptides
show the reaction diagram
additional information
?
-
-
adipocytes/pre-adipocytes and MMP-11 participate in a highly complex vicious cycle to support tumor progression, and this process is orchestrated by cancer cells. First, both invasive cancer cells and resting adipocytes/pre-adipocytes do not express MMP-11. When a cancer cell meets an adipocyte/pre-adipocyte, their cross-talk/interaction induces the expression/secretion of MMP-11 by the adipocyte/pre-adipocyte. MMP-11 negatively regulates adipogenesis, leading to a decrease in adipocyte differentiation and accumulation/maintenance of MMP-11-expressing fibroblast like cells. These latter cells then act on adjacent invasive cancer cells to favor their survival and potentiate this vicious cycle
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
matrix metalloprotease inhibitor TIMP-2
-
-
-
matrix metalloproteinase inhibitor AG3340
-
broad spectrum inhibitor
matrix metalloproteinase inhibitor BB-94
-
-
matrix metalloproteinase inhibitor TIMP-2
-
-
-
additional information
-
no inhibition by aprotinin
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.294 - 0.705
GGAANLVRGG
0.148 - 0.207
GGYAELRMGG
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.69 - 6.08
GGAANLVRGG
0.58 - 6.08
GGYAELRMGG
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000006
matrix metalloproteinase inhibitor AG3340
-
pH 7.6, 37°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
substrate specificity
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
-
assay at
7.5 - 7.6
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
usage of microarray analysis to compare the variations of gene expression within the papillary thyroid carcinoma (PTC) cell populations and their adjacent normal tissues, MMP-11 is the most differentially expressed matrix metalloproteinase, MMP. MMP-11 expression is upregulated in PTC. The change in cyclin D1 is consistent with MMP-11 expression, which may explain the changes in proliferation
Manually annotated by BRENDA team
-
increased expression of MMP11 at mRNA and protein levels in cell lines and primary tumors of gastric cancer. Overexpression of MMP11 induced proliferation and invasion in AGS cells
Manually annotated by BRENDA team
-
MMP11 protein is frequently detected in sera of common cancer patients including gastric cancer
Manually annotated by BRENDA team
-
ST-3+/TIMP-2- (stromelysin-3+/matrix metalloproteinase TIMP-2)-phenotype is an adverse prognosticator in esophageal cancer patients
Manually annotated by BRENDA team
-
BGC823. MMP11 may play an important role in the control of cell proliferation and tumor development in gastric cancer
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
the levels of proliferation and migration of cells transfected with MMP-11 siRNA are significantly reduced, while the levels in MMP-11-plasmid-transfected cells are increased. Variations in intracellular MMP-11 significantly alters the amount of phospho-p65 in thyroid cells, while p65 knockdown does not affect MMP-11 expression
metabolism
physiological function
malfunction
physiological function
-
MMP-11 plays a role in lobular carcinogenesis through increasing resistance to anoikis
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
MMP11_HUMAN
488
0
54590
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22000
-
x * 22000, recombinant processed and truncated form, SDS-PAGE
44000
-
x * 44000, active processed form, SDS-PAGE
50000
55000
-
x * 55000, proenzyme form, SDS-PAGE
60000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
MMP-11 possesses a furin recognition motif RXKR, but it lacks the C-terminal transmembrane domain of MMPs
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A38V
polymorphismsm rs738792, T/C, may be associated with Kawazaki disease in the Korean population
A235P
E216A
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant catalytic domain and mutants from Escherichia coli
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene MMP11, quantitative enzyme expression analysis
gene MMP11, quantitative real-time PCR enzyme expression analysis
expressed in COS-7 and MDA-MB-330 cells
-
expressed in MCF-7 cells and MDA-MB-231 cells
-
expression in MCF-7 breat adenocarcinoma cells, secretion of the enzyme
-
expression of catalytic site comprising residues 98-272 and of mutants A235P and E216A in Escherichia coli
-
expression of truncated mutant lacking the N-terminal prodomain, the C-terminal part of the hemopexin-like domain, and mutant A235P in Escherichia coli BL21(DE3)
-
MMP-11 expression analysis
-
MMP11, expression analysis
-
MP-11 expression analysis
-
overexpression of wild-type and mutant E220A in Escherichia coli, expression of wild-type and inactive enzyme in MCF7 carcinoma cells
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
MMP-11 expression is upregulated in papillary thyroid carcinoma
treatment of BCS-TC2 cells with butyrate and trichostatin A (histone deacetylase inhibitors) increases MMP11 promoter activity 1.5-2fold and protein expression 1.4-1.7fold. Sp1 is involved in MMP11 basal expression and is essential for the upregulation of transcription by histone deacetylase inhibitors. ERK1/2-mitogen-activated protein kinase, but not p38-MAPK or JNK, is involved in the upregulation of MMP11 by histone deacetylase inhibitors
-
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
mutant enzyme are solubilized and refolded from inclusion bodies after expression in Escherichia coli
-
refolding of recombinant enzyme from inclusion bodies after overexpression in Escherichia coli
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
diagnostics
medicine
enzyme MMP-11 is an antigen target for immunotherapy
diagnostics
medicine
pharmacology
-
enzyme form with the specific residue A235 is an attractive target for the development of specific inhibitors for use in prevention of cancer progression
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 (P24347), Xenopus laevis (Q11005)
Manually annotated by BRENDA team
Noel, A.; Santavicca, M.; Stoll, I.; L'Hoir, C.; Staub, A.; Murphy, G.; Rio, M.C.; Basset, P.
Identification of structural determinants controlling human and mouse stromelysin-3 proteolytic activities
J. Biol. Chem.
270
22866-22872
1995
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Manes, S.; Mira, E.; Barbacid, M.M.; Cipres, A.; Fernandez-Resa, P.; Buesa, J.M.; Merida, I.; Aracil, M.; Marquez, G.; Martinez, A.C.
Identification of insulin-like growth factor-binding protein-1 as a potential physiological substrate for human stromelysin-3
J. Biol. Chem.
272
25706-25712
1997
Homo sapiens
Manually annotated by BRENDA team
Pan, W.; Arnone, M.; Kendall, M.; Grafstrom, R.H.; Seitz, S.P.; Wasserman, Z.R.; Albright, C.F.
Identification of peptide substrates for human MMP-11 (stromelysin-3) using phage display
J. Biol. Chem.
278
27820-27827
2003
Homo sapiens
Manually annotated by BRENDA team
Noel, A.; Boulay, A.; Kebers, F.; Kannan, R.; Hajitou, A.; Calberg-Bacq, C.M.; Basset, P.; Rio, M.C.; Foidart, J.M.
Demonstration in vivo that stromelysin-3 functions through its proteolytic activity
Oncogene
19
1605-1612
2000
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Deng, H.; Guo, R.F.; Li, W.M.; Zhao, M.; Lu, Y.Y.
Matrix metalloproteinase 11 depletion inhibits cell proliferation in gastric cancer cells
Biochem. Biophys. Res. Commun.
326
274-281
2005
Homo sapiens
Manually annotated by BRENDA team
Andarawewa, K.L.; Motrescu, E.R.; Chenard, M.P.; Gansmuller, A.; Stoll, I.; Tomasetto, C.; Rio, M.C.
Stromelysin-3 is a potent negative regulator of adipogenesis participating to cancer cell-adipocyte interaction/crosstalk at the tumor invasive front
Cancer Res.
65
10862-10871
2005
Homo sapiens
Manually annotated by BRENDA team
Sharma, R.; Chattopadhyay, T.K.; Mathur, M.; Ralhan, R.
Prognostic significance of stromelysin-3 and tissue inhibitor of matrix metalloproteinase-2 in esophageal cancer
Oncology
67
300-309
2004
Homo sapiens
Manually annotated by BRENDA team
Kasper, G.; Reule, M.; Tschirschmann, M.; Dankert, N.; Stout-Weider, K.; Lauster, R.; Schrock, E.; Mennerich, D.; Duda, G.N.; Lehmann, K.E.
Stromelysin-3 over-expression enhances tumourigenesis in MCF-7 and MDA-MB-231 breast cancer cell lines: involvement of the IGF-1 signalling pathway
BMC Cancer
7
12
2007
Homo sapiens
Manually annotated by BRENDA team
Kim, H.J.; Lee, J.Y.; Kim, S.H.; Seo, Y.J.; Lee, J.H.; Park, J.K.; Kim, M.H.; Cinn, Y.W.; Cho, K.H.; Yoon, T.Y.
Stromelysin-3 expression in the differential diagnosis of dermatofibroma and dermatofibrosarcoma protuberans: comparison with factor XIIIa and CD34
Br. J. Dermatol.
157
319-324
2007
Homo sapiens
Manually annotated by BRENDA team
Motrescu, E.R.; Rio, M.C.
Cancer cells, adipocytes and matrix metalloproteinase 11: a vicious tumor progression cycle
Biol. Chem.
389
1037-1041
2008
Homo sapiens
Manually annotated by BRENDA team
Yang, Y.H.; Deng, H.; Li, W.M.; Zhang, Q.Y.; Hu, X.T.; Xiao, B.; Zhu, H.H.; Geng, P.L.; Lu, Y.Y.
Identification of matrix metalloproteinase 11 as a predictive tumor marker in serum based on gene expression profiling
Clin. Cancer Res.
14
74-81
2008
Homo sapiens
Manually annotated by BRENDA team
Motrescu, E.R.; Blaise, S.; Etique, N.; Messaddeq, N.; Chenard, M.P.; Stoll, I.; Tomasetto, C.; Rio, M.C.
Matrix metalloproteinase-11/stromelysin-3 exhibits collagenolytic function against collagen VI under normal and malignant conditions
Oncogene
27
6347-6355
2008
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Mathew, S.; Fu, L.; Hasebe, T.; Ishizuya-Oka, A.; Shi, Y.B.
Tissue-dependent induction of apoptosis by matrix metalloproteinase stromelysin-3 during amphibian metamorphosis
Birth Defects Res. C Embryo Today
90
55-66
2010
Homo sapiens, Mus musculus, Xenopus laevis
Manually annotated by BRENDA team
Peruzzi, D.; Mori, F.; Conforti, A.; Lazzaro, D.; De Rinaldis, E.; Ciliberto, G.; La Monica, N.; Aurisicchio, L.
MMP11: a novel target antigen for cancer immunotherapy
Clin. Cancer Res.
15
4104-4113
2009
Homo sapiens, Mus musculus, Mus musculus BALB/c
Manually annotated by BRENDA team
Cheng, C.W.; Yu, J.C.; Wang, H.W.; Huang, C.S.; Shieh, J.C.; Fu, Y.P.; Chang, C.W.; Wu, P.E.; Shen, C.Y.
The clinical implications of MMP-11 and CK-20 expression in human breast cancer
Clin. Chim. Acta
411
234-241
2010
Homo sapiens
Manually annotated by BRENDA team
Zhao, Z.S.; Chu, Y.Q.; Ye, Z.Y.; Wang, Y.Y.; Tao, H.Q.
Overexpression of matrix metalloproteinase 11 in human gastric carcinoma and its clinicopathologic significance
Hum. Pathol.
41
686-696
2010
Homo sapiens
Manually annotated by BRENDA team
Ban, J.Y.; Kim, S.K.; Kang, S.W.; Yoon, K.L.; Chung, J.H.
Association between polymorphisms of matrix metalloproteinase 11 (MMP-11) and Kawasaki disease in the Korean population
Life Sci.
86
756-759
2010
Homo sapiens (P24347), Homo sapiens
Manually annotated by BRENDA team
Barrasa, J.I.; Olmo, N.; Santiago-Gomez, A.; Lecona, E.; Anglard, P.; Turnay, J.; Lizarbe, M.A.
Histone deacetylase inhibitors upregulate MMP11 gene expression through Sp1/Smad complexes in human colon adenocarcinoma cells
Biochim. Biophys. Acta
1823
570-581
2012
Homo sapiens
Manually annotated by BRENDA team
Takeuchi, T.; Adachi, Y.; Nagayama, T.; Furihata, M.
Matrix metalloproteinase-11 overexpressed in lobular carcinoma cells of the breast promotes anoikis resistance
Virchows Arch.
459
291-297
2011
Homo sapiens
Manually annotated by BRENDA team
Gonzalez de Vega, R.; Clases, D.; Fernandez-Sanchez, M.L.; Eiro, N.; Gonzalez, L.O.; Vizoso, F.J.; Doble, P.A.; Sanz-Medel, A.
MMP-11 as a biomarker for metastatic breast cancer by immunohistochemical-assisted imaging mass spectrometry
Anal. Bioanal. Chem.
411
639-646
2019
Homo sapiens (P24347), Homo sapiens
Manually annotated by BRENDA team
Zhang, X.; Huang, S.; Guo, J.; Zhou, L.; You, L.; Zhang, T.; Zhao, Y.
Insights into the distinct roles of MMP-11 in tumor biology and future therapeutics (Review)
Int. J. Oncol.
48
1783-1793
2016
Homo sapiens (P24347), Homo sapiens
Manually annotated by BRENDA team
Zhang, Z.; Dong, T.; Fu, Y.; Zhou, W.; Tian, X.; Chen, G.; Liu, S.
MMP-11 promotes papillary thyroid cell proliferation and invasion via the NF-kappaB pathway
J. Cell. Biochem.
120
1860-1868
2019
Homo sapiens (P24347)
Manually annotated by BRENDA team
Hsin, C.H.; Chou, Y.E.; Yang, S.F.; Su, S.C.; Chuang, Y.T.; Lin, S.H.; Lin, C.W.
MMP-11 promoted the oral cancer migration and Fak/Src activation
Oncotarget
8
32783-32793
2017
Homo sapiens (P24347), Homo sapiens
Manually annotated by BRENDA team