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Information on EC 3.4.24.B9 - ADAM9 endopeptidase and Organism(s) Mus musculus and UniProt Accession Q61072

for references in articles please use BRENDA:EC3.4.24.B9
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.B9 ADAM9 endopeptidase
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This record set is specific for:
Mus musculus
UNIPROT: Q61072
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Word Map
The taxonomic range for the selected organisms is: Mus musculus
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
proteolytic degradation of proteins
Synonyms
adam9, adam-9, adam 9, mdc-9, meltrin gamma, adam metallopeptidase domain 9, meltrin-gamma, a disintegrin and metalloproteinase domain 9, mdc9/meltrin-gamma/adam9, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
cellular disintegrin-related protein
precursor
M12.209
Merops-ID
meltrin gamma
-
ADAM 9
-
-
ADAM metallopeptidase domain 9
-
-
M12.209
-
Merops-ID
MDC9/meltrin-gamma/ADAM9
-
-
meltrin gamma
-
-
meltrin-gamma
-
-
metallo protease desintegrin 9
-
-
metalloprotease ADAM9
-
-
metalloprotease disintegrin 9
-
-
additional information
-
ADAM9 is a widely expressed and particularly polyvalent member of the multifunctional ADAM family of proteins
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
hydrolysis of peptide bond
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
252565-22-3
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ephrin receptor B4 + H2O
?
show the reaction diagram
-
-
-
?
proteins + H2O
peptides
show the reaction diagram
-
-
?
ADAM10 + H2O
?
show the reaction diagram
-
shedding of the ectodomain of ADAM10
-
-
?
amyloid precursor protein + H2O
90-100 kDa non-amyloid N-terminal protein fragment
show the reaction diagram
-
alpha-secretase activity
-
?
amyloid precursor protein + H2O
?
show the reaction diagram
-
-
-
-
?
beta-casein + H2O
?
show the reaction diagram
-
-
-
-
?
EVHHQKLVFFAE + H2O
EVHH + QKLVFFAE
show the reaction diagram
-
peptides derived from beta-amyloid precursor protein, comprises the predicted cleavage site
-
?
Fibronectin + H2O
?
show the reaction diagram
-
-
-
-
?
Gelatin + H2O
?
show the reaction diagram
-
-
-
-
?
heparin-binding EGF-like growth factor + H2O
heparin-binding EGF-like growth factor fragment
show the reaction diagram
-
cooperative action with bound protein kinase C, membrane-anchored substrate, ectodomain shedding
soluble product
?
insulin B chain + H2O
3 peptides
show the reaction diagram
-
cleavage sites are Tyr16-Leu17 and Tyr26-Thr27
-
?
insulin B chain + H2O
?
show the reaction diagram
-
-
-
-
?
pro-heparin-binding EGF-like growth factor + H2O
?
show the reaction diagram
proteins + H2O
peptides
show the reaction diagram
SMAPGAVHLPQP + H2O
SMAPGAVH + LPQP
show the reaction diagram
-
peptides derived from P75 TNF-receptor, comprises the predicted cleavage site
-
?
SPLAQAVRSSSR + H2O
SPLA + QAVRSSSR
show the reaction diagram
-
peptides derived from TNF-alpha, comprises the predicted cleavage site
-
?
SPLAQAVRSSSR + H2O
SPLAQAVRS + SSR
show the reaction diagram
-
peptides derived from TNF-alpha, comprises the predicted cleavage site
-
?
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
proteins + H2O
peptides
show the reaction diagram
-
-
?
heparin-binding EGF-like growth factor + H2O
heparin-binding EGF-like growth factor fragment
show the reaction diagram
-
cooperative action with bound protein kinase C, membrane-anchored substrate, ectodomain shedding
soluble product
?
pro-heparin-binding EGF-like growth factor + H2O
?
show the reaction diagram
-
cooperative action with bound protein kinase C, membrane-anchored substrate, ectodomain shedding
-
?
proteins + H2O
peptides
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mn2+
-
metalloprotease
additional information
-
metalloprotease
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
batimastat
-
GM6001
hydroxamate inhibitor
GW280264X
-
marimastat
-
TAPI-2
hydroxamate inhibitor
TIMP-3
i.e. tissue inhibitor of metalloproteinases-3, inhibition at 10 nM
-
1,10-phenanthroline
-
-
batimastat
-
-
brefeldin A
-
blocks processing of the enzyme precursor by blocking the vesicle budding in the endoplasmic reticulum
CGS 27023
-
-
coban
-
complete blockage of enzyme processing at 0.025 mg/ml
marimastat
-
-
metalloprotease inhibitor SI-27
-
-
-
PKVCGYLK
-
inhibition less tan 20% at 0.1 mM
PLKCGVSN
-
inhibition less tan 20% at 0.1 mM
PLRCGVSN
-
inhibition less tan 20% at 0.1 mM
QGGCADHS
-
inhibition less tan 20% at 0.1 mM
QGLCGSQH
-
inhibition less tan 20% at 0.1 mM
TNF-alpha protease inhibitor
-
-
-
additional information
not inhibitory: up to 20 nM of TIMP-1 or -2
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
phorbol myristate acetate ester
-
-
Protein kinase C
-
additional information
ADAM9 does not respond to stimulation with phorbol esters, calcium ionophore or phosphatase inhibitors
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000014
batimastat
-
pH 7.5
0.000054
CGS 27023
-
pH 7.5
0.00027
marimastat
-
pH 7.5
0.004
PKVCGYLK
-
pH 7.5
0.037
PLKCGVSN
-
pH 7.5
0.01
PLRCGVSN
-
pH 7.5
0.15
QGGCADHS
-
pH 7.5
0.15
QGLCGSQH
-
pH 7.5
0.000017
TNF-alpha protease inhibitor
-
pH 7.5
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00005
batimastat
Mus musculus
pH not specified in the publication, temperature not specified in the publication
0.00072
GM6001
Mus musculus
pH not specified in the publication, temperature not specified in the publication
0.00048
GW280264X
Mus musculus
pH not specified in the publication, temperature not specified in the publication
0.00013
marimastat
Mus musculus
pH not specified in the publication, temperature not specified in the publication
0.0135
TAPI-2
Mus musculus
pH not specified in the publication, temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.2
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
-
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
study on expression patterns of enzymes ADAM9, ADAM10, and ADAM 17 during pancreas ontogeny. The three enzymes are expressed in the pancreas anlagen. During development, ADAM9 becomes restricted to the insulin-producing beta-cells
Manually annotated by BRENDA team
-
apical surface of the retinal pigment epithelium
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
ADAM9 localises to cell-cell junctions and colocalises with cell-cell junction proteins in endothelial cells. Expression is required in two adjacent cells for localisation to cell-cell junctions. ADAM9 can self-associate through ectodomain interactions. The soluble ADAM9 ectodomain cannot increase endothelial monolayer permeability or inhibit monocyte-endothelial adhesion, but can inhibit monocyte-endothelial transmigration
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
coculture of melanoma cells in the presence of ADAM-9-/- fibroblasts leads to increased melanoma cell proliferation and reduced apoptosis as compared with control cocultures. TIMP-1 and sTNFRI are the two relevant factors expressed in increased amounts in culture supernatants from ADAM-9-/- fibroblasts. TIMP-1 is associated with induced melanoma cell proliferation, whereas soluble TNFR1 mediates the reduced cellular apoptosis in vitro. In vivo, injection of murine melanoma cells into the flank of ADAM-9-/- animals results in the development of significantly larger tumors than in wild-type animals as a result of increased proliferation and decreased apoptosis of melanoma cells
physiological function
additional information
-
ADAM9 is a widely expressed and particularly polyvalent member of the multifunctional ADAM family of proteins
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ADAM9_MOUSE
845
0
92079
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
12000
-
x * 84000, processed enzyme, x * 12000, enzyme proform, SDS-PAGE
84000
-
x * 84000, processed enzyme, x * 12000, enzyme proform, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 84000, processed enzyme, x * 12000, enzyme proform, SDS-PAGE
additional information
-
constitutive interaction of enzyme with E-cadherin
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
-
N-glycosylation of endopeptidase H-sensitive precursor and mature enzyme
proteolytic modification
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant soluble enzyme from COS-7 cells
-
recombinant wild-type and mutant from COS-7 cells
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in COS-7 cell
expressed in COS cells
-
expression of FLAG-tagged enzyme in COS-7 cells
-
expression of GST-linked cytoplasmic region in Escherichia coli, coeexpression of the enzyme and protein kinase C in COS-7 cells, overexpression of wild-type and deletion mutants in Vero-H cells
-
expression of Sec-tagged wild-type and metalloprotease domain deletion mutant in COS-7 cells
-
expression of soluble enzyme form, nucleotides 1-1253, with a Myc-epitope in COS-7 cells
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
injection of murine melanoma cells into the flank of ADAM-9-/- animals resultsin the development of significantly larger tumors than in wild-type animals as a result of increased proliferation and decreased apoptosis of melanoma cells
medicine
-
enzyme overexpression in A-549 and EBC-1 cells results in increased invasive capacity in response to nerve growth factor, increased adhesion to brain tissue, and increased expression of integrin alpha3 and beta1 subunits. Administration of enzyme overexpressing A-549 cells to mice results in micrometastatic foci in brain and multiple metastatic colonies in the lungs
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 (Q13443), Mus musculus (Q61072)
Manually annotated by BRENDA team
Koike, H.; Tomioka, S.; Sorimachi, H.; Saido, T.C.; Maruyama, K.; Okuyama, A.; Fujisawa-Sehara, A.; Ohno, S.; Suzuki, K.; Ishiura, S.
Membrane-anchored metalloprotease MDC9 has an alpha-secretase activity responsible for processing the amyloid precursor protein
Biochem. J.
343
371-375
1999
Mus musculus
Manually annotated by BRENDA team
Izumi, Y.; Hirata, M.; Hasuwa, H.; Iwamoto, R.; Umata, T.; Miyado, K.; Tamai, Y.; Kurisaki, T.; Sehara-Fujisawa, A.; Ohno, S.; Mekada, E.
A metalloprotease-disintegrin, MDC9/meltrin-gamma/ADAM9 and PKCdelta are involved in TPA-induced ectodomain shedding of membrane-anchored heparin-binding EGF-like growth factor
EMBO J.
17
7260-7272
1998
Mus musculus
Manually annotated by BRENDA team
Howard, L.; Nelson, K.K.; Maciewicz, R.A.; Blobel, C.P.
Interaction of the metalloprotease disintegrins MDC9 and MDC15 with two SH3 domain-containing proteins, endophilin I and SH3PX1
J. Biol. Chem.
274
31693-31699
1999
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Roghani, M.; Becherer, J.D.; Moss, M.L.; Atherton, R.E.; Erdjument-Bromage, H.; Arribas, J.; Blackburn, R.K.; Weskamp, G.; Tempst, P.; Blobel, C.P.
Metalloprotease-disintegrin MDC9: intracellular maturation and catalytic activity
J. Biol. Chem.
274
3531-3540
1999
Mus musculus
Manually annotated by BRENDA team
Mahimkar, R.M.; Visaya, O.; Pollock, A.S.; Lovett, D.H.
The disintegrin domain of ADAM9: a ligand for multiple b1 renal integrins
Biochem. J.
385
461-468
2005
Mus musculus
Manually annotated by BRENDA team
Shintani, Y.; Higashiyama, S.; Ohta, M.; Hirabayashi, H.; Yamamoto, S.; Yoshimasu, T.; Matsuda, H.; Matsuura, N.
Overexpression of ADAM9 in non-small cell lung cancer correlates with brain metastasis
Cancer Res.
64
4190-4196
2004
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Peduto, L.; Reuter, V.E.; Shaffer, D.R.; Scher, H.I.; Blobel, C.P.
Critical function for ADAM9 in mouse prostate cancer
Cancer Res.
65
9312-9319
2005
Mus musculus
Manually annotated by BRENDA team
Asayesh, A.; Alanentalo, T.; Khoo, N.K.; Ahlgren, U.
Developmental expression of metalloproteases ADAM 9, 10, and 17 becomes restricted to divergent pancreatic compartments
Dev. Dyn.
232
1105-1114
2005
Mus musculus
Manually annotated by BRENDA team
Hirao, T.; Nanba, D.; Tanaka, M.; Ishiguro, H.; Kinugasa, Y.; Doki, Y.; Yano, M.; Matsuura, N.; Monden, M.; Higashiyama, S.
Overexpression of ADAM9 enhances growth factor-mediated recycling of E-cadherin in human colon cancer cell line HT29 cells
Exp. Cell Res.
312
331-339
2006
Mus musculus
Manually annotated by BRENDA team
Deuss, M.; Reiss, K.; Hartmann, D.
Part-time alpha-secretases: the functional biology of ADAM 9, 10 and 17
Curr. Alzheimer Res.
5
187-201
2008
Mus musculus
Manually annotated by BRENDA team
Parry, D.A.; Toomes, C.; Bida, L.; Danciger, M.; Towns, K.V.; McKibbin, M.; Jacobson, S.G.; Logan, C.V.; Ali, M.; Bond, J.; Chance, R.; Swendeman, S.; Daniele, L.L.; Springell, K.; Adams, M.; Johnson, C.A.; Booth, A.P.; Jafri, H.; Rashid, Y.; Banin, E.; Strom, T.M.; Farber, D.B.; Sharon, D.; Blobel, C.P.; Pugh, E.
Loss of the metalloprotease ADAM9 leads to cone-rod dystrophy in humans and retinal degeneration in mice
Am. J. Hum. Genet.
84
683-691
2009
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Abety, A.N.; Fox, J.W.; Schoenefuss, A.; Zamek, J.; Landsberg, J.; Krieg, T.; Blobel, C.; Mauch, C.; Zigrino, P.
Stromal fibroblast-specific expression of ADAM-9 modulates proliferation and apoptosis in melanoma cells in vitro and in vivo
J. Invest. Dermatol.
132
2451-2458
2012
Mus musculus (Q61072), Mus musculus
Manually annotated by BRENDA team
Wang, X.; Polverino, F.; Rojas-Quintero, J.; Zhang, D.; Sánchez, J.; Yambayev, I.; Lindqvist, E.; Virtala, R.; Djukanovic, R.; Davies, D.; Wilson, S.; ODonnell, R.; Cunoosamy, D.; Hazon, P.; Higham, A.; Singh, D.; Olsson, H.; Owen, C.
A disintegrin and metalloproteinase domain-9 A novel proteinase culprit with multifarious contributions to chronic obstructive pulmonary disease
Am. J. Respir. Crit. Care Med.
198
1500-1518
2018
Mus musculus, Homo sapiens (Q13443)
-
Manually annotated by BRENDA team
English, W.; Siviter, R.; Hansen, M.; Murphy, G.
ADAM9 is present at endothelial cell - cell junctions and regulates monocyte - endothelial transmigration
Biochem. Biophys. Res. Commun.
493
1057-1062
2017
Mus musculus (Q61072)
Manually annotated by BRENDA team
Maretzky, T.; Swendeman, S.; Mogollon, E.; Weskamp, G.; Sahin, U.; Reiss, K.; Blobel, C.
Characterization of the catalytic properties of the membrane-anchored metalloproteinase ADAM9 in cell-based assays
Biochem. J.
474
1469-1479
2017
Mus musculus (Q61072)
Manually annotated by BRENDA team