3.4.24.81: ADAM10 endopeptidase
This is an abbreviated version!
For detailed information about ADAM10 endopeptidase, go to the full flat file.
Word Map on EC 3.4.24.81
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3.4.24.81
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alzheimer
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adam17
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amyloid
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ectodomain
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sheddase
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alpha-secretase
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endothelial
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metalloproteases
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neuroprotective
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plaque
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amyloidogenic
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non-amyloidogenic
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tnf
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sh-sy5y
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synaptic
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secretase
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membrane-anchored
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tetraspanins
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gamma-secretase
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n-cadherin
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presenilins
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notch1
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intramembrane
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abeta
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cxcl16
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prpc
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prion
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amyloid-beta
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prodomains
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psen1
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beta-secretase
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sappalpha
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hb-egf
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beta-site
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trans-signaling
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amphiregulin
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fractalkine
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meprin
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disintegrin-like
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adam17-mediated
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app-cleaving
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betacellulin
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nicastrin
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timp-3
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molecular biology
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anti-amyloidogenic
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medicine
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srage
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notch-dependent
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ad-like
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juxtamembrane
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bace-1
- 3.4.24.81
- alzheimer
- adam17
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amyloid
- ectodomain
- sheddase
- alpha-secretase
- endothelial
- metalloproteases
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neuroprotective
- plaque
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amyloidogenic
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non-amyloidogenic
- tnf
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sh-sy5y
- synaptic
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secretase
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membrane-anchored
- tetraspanins
- gamma-secretase
- n-cadherin
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presenilins
- notch1
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intramembrane
- abeta
- cxcl16
- prpc
- prion
- amyloid-beta
- prodomains
- psen1
- beta-secretase
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sappalpha
- hb-egf
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beta-site
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trans-signaling
- amphiregulin
- fractalkine
- meprin
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disintegrin-like
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adam17-mediated
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app-cleaving
- betacellulin
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nicastrin
- timp-3
- molecular biology
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anti-amyloidogenic
- medicine
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srage
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notch-dependent
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ad-like
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juxtamembrane
- bace-1
Reaction
endopeptidase of broad specificity =
Synonyms
a disintegrin and metalloprotease 10, a disintegrin and metalloproteinase 10, a disintegrin and metalloproteinase-10, a-disintegrin-and-metalloprotease 10, AD10, ADAM 10, ADAM-10, ADAM10, CD156c, CD23 metalloprotease, HsT18717, kuz, kuzbanian, Kuzbanian protein, MADM, mammalian disintegrin-metalloprotease, metalloproteinase 10, metalloproteinase ADAM10, metalloproteinase Kuzbanian, metalloproteinase MADM, metalloproteinase-disintegrin, myelin-associated disintegrin metalloproteinase, notch proteinase, transmembrane metzinkin-protease of the a disintegrin and metalloproteinase family-10
ECTree
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Natural Substrates Products
Natural Substrates Products on EC 3.4.24.81 - ADAM10 endopeptidase
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REACTION DIAGRAM
beta-amyloid precursor protein + H2O
sAPP-alpha fragment of beta-amyloid precursor protein + C-terminal fragment of beta-amyloid precursor protein
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?
collagen XVII/BP180 + H2O
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ADAM9 and ADAM10 are the most prominent collagen XVII sheddases in primary keratinocytes
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-
?
epithelial growth factor receptor
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activation of the receptor leads to cleavage of transmembrane heparin-binding site by ADAM10 in response to infection by Staphylococcus aureus
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?
FcalphaR + H2O
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FcaR (CD89) is the Fc receptor for immunoglobulin A. ADAM10 and ADAM17 are involved in the shedding of FcalphaR
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?
interleukin-6 receptor + H2O
sIL-6R fragment + C-terminal fragment
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?
L-selectin + H2O
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ADAMs 10 and 17 represent differentially regulated components of a general shedding machinery for membrane proteins such as transforming growth factor alpha, L-selectin, and tumor necrosis factor alpha
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?
L1 adhesion molecule
L1-200 fragment + L1-32 fragment + ?
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ADAM10 cleaves L1
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?
L1 cell-adhesion molecule + H2O
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the ectodomain of L1 cell-adhesion molecule is cleaved at the plasma membrane by ADAM10. Regulated proteolytic processing by ADAM10 and PS/gamma-secretase is essential for the nuclear signalling of L1 in human carcinoma cell lines
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?
Notch S2 + H2O
Notch extracellular truncation fragment + ?
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the enzyme is responsible for proteolytic cleavage at the S2 cleavage site within the extracellular juxtamembrane region of the Notch C-terminal fragment, which leads to the removal of the Notch ectodomain and the generation of a membrane-anchored Notch C-terminal fragment, termed Notch extracellular truncation
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?
transforming growth factor alpha + H2O
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ADAMs 10 and 17 represent differentially regulated components of a general shedding machinery for membrane proteins such as transforming growth factor alpha, L-selectin, and tumor necrosis factor alpha
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?
tumor necrosis factor alpha + H2O
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ADAMs 10 and 17 represent differentially regulated components of a general shedding machinery for membrane proteins such as transforming growth factor alpha, L-selectin, and tumor necrosis factor alpha
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?
?
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cleaves amyloid precursor protein in its transmembrane region alpha-secretase activity
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?
amyloid precursor protein + H2O
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tetraspanin12 associates with mature ADAM10, promotes ADAM10 maturation, and enhances ADAM10 dependent cleavage of amyloid precursor protein
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?
amyloid precursor protein + H2O
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ADAM10 plays a central role in the developing brain by controlling mainly Notch-dependent pathways but likely also by reducing surface shedding of other neuronal membrane proteins including amyloid precursor protein
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?
amyloid precursor protein + H2O
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cleaves amyloid precursor protein in its transmembrane region alpha-secretase activity
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?
annexin A1 + H2O
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ADAM10 cleaves within the N-terminal domain after Phe7, cleavage occurs on the outer cell surface during secondary but not primary necrosis
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sAPP-alpha fragment + C-terminal fragment
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beta-amyloid precursor protein
sAPP-alpha fragment + C-terminal fragment
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?
beta-amyloid precursor protein
sAPP-alpha fragment + C-terminal fragment
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A172 cell line has alpha-secretase activity
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?
beta-amyloid precursor protein
sAPP-alpha fragment + C-terminal fragment
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LoVo cell line overexpressing ADAM10 secreted a 185% of sAPP-alpha over control values
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?
beta-amyloid precursor protein
sAPP-alpha fragment + C-terminal fragment
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platelet and cerebrospinal fluid have lower levels of alpha-APP in Alzheimer patients
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?
sAPP-alpha fragment + C-terminal fragment
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?
beta-amyloid precursor protein + H2O
sAPP-alpha fragment + C-terminal fragment
cleavage at Lys683-Leu684
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?
beta-amyloid precursor protein + H2O
sAPP-alpha fragment + C-terminal fragment
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?
N1 fragment + C-terminal fragment
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constitutive protein cleavage
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?
cellular prion protein
N1 fragment + C-terminal fragment
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constitutive protein cleavage
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?
cellular prion protein
N1 fragment + C-terminal fragment
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knock out line has 51% of reduction in N1 formation
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?
E-cadherin + H2O
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efficient cleavage of the ADAM10 substrate epithelial cadherin (E-cadherin) requires supra-cytotoxic concentrations of alpha-toxin
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?
?
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ADAM10 is required for site 2 cleavage of the single-pass transmembrane receptor Notch1
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Notch1 + H2O
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ADAM10 plays a central role in the developing brain by controlling mainly Notch-dependent pathways but likely also by reducing surface shedding of other neuronal membrane proteins including amyloid precursor protein
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Notch1 + H2O
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although Notch1 is a substrate for both ADAM10 and ADAM17, the particular ADAM required for receptor activation is context dependent. Specifically, ADAM10 is absolutely required for Notch1 signaling induced by ligands. Noth proteases participated in signaling intrinsic to Notch1 mutations associated with leukemia
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?
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TIMP1 and TIMP-3 (tissue inhibitors of metalloproteinase) interact and inhibit ADAM10
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additional information
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the enzyme can cut normal prion proteins from the surface of neurons
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?