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Information on EC 3.4.24.81 - ADAM10 endopeptidase and Organism(s) Bos taurus

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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.24 Metalloendopeptidases
                3.4.24.81 ADAM10 endopeptidase
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This record set is specific for:
Bos taurus
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Word Map
The taxonomic range for the selected organisms is: Bos taurus
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
endopeptidase of broad specificity
Synonyms
adam10, adam-10, adam 10, a disintegrin and metalloproteinase 10, a disintegrin and metalloprotease 10, kuzbanian, metalloproteinase adam10, metalloproteinase 10, metalloproteinase-disintegrin, a disintegrin and metalloproteinase-10, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
a disintegrin and metalloprotease 10
-
-
ADAM-10
-
-
-
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Kuzbanian protein
-
-
-
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mammalian disintegrin-metalloprotease
-
-
-
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metalloproteinase ADAM10
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-
-
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metalloproteinase Kuzbanian
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-
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metalloproteinase MADM
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-
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myelin-associated disintegrin metalloproteinase
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-
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notch proteinase
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
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-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
193099-09-1
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
Abz-Leu-Ala-Gln-Ala-Val-Arg-Ser-Ser-Ser-Arg-Dap(dnp)-NH2 + H2O
?
show the reaction diagram
-
-
-
-
?
beta-amyloid precursor protein
sAPP-alpha fragment + C-terminal fragment
show the reaction diagram
-
-
-
-
?
ephrin-A2 + H2O
?
show the reaction diagram
-
-
-
-
?
ephrin-A5 + H2O
?
show the reaction diagram
-
-
-
-
?
L1 cell adhesion molecule + H2O
?
show the reaction diagram
-
-
-
-
?
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
beta-amyloid precursor protein
sAPP-alpha fragment + C-terminal fragment
show the reaction diagram
-
-
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
-
inhibits shedding of Eph-A5
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ADA10_BOVIN
748
1
84188
Swiss-Prot
Secretory Pathway (Reliability: 1)
A0A452DJA5_BOVIN
680
1
76296
TrEMBL
other Location (Reliability: 4)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
62000 - 64000
-
active form, amino-terminal sequencing
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
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contains high-mannose as well as complex-type N-glycans. Glycosylation sites: S269, T280, S441, T553
proteolytic modification
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the enzyme has an inactive form that is activated by cleavage
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging-drop vapour diffusion
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
S269A
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mutant is detected at lower molecular masses than the wild-type form, which indicates that the N-glycosylation site is occupied
S441A
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mutant is detected at lower molecular masses than the wild-type form, which indicates that the N-glycosylation site is occupied, mutant shows increased ADAM10 susceptibility to proteolysis
T280A
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mutant is detected at lower molecular masses than the wild-type form, which indicates that the N-glycosylation site is occupied, T280A is found to accumulate in the endoplasmic reticulum as the non-processed precursor of the enzyme. Mutant exhibits only residual levels of metalloprotease activity
T553A
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mutant is detected at lower molecular masses than the wild-type form, which indicates that the N-glycosylation site is occupied
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
SDS-PAGE
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
a C-terminal HA-tagged fusion protein is transfected in human ovarian cancer SKOV3 cells and human embryonic kidney HEK293 cells
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expressed in HEK-293 cells
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expressed in human embryonic kidney HEK293 cell line
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
molecular biology
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there is only a moderate alteration of gene expression in ADAM10 overexpressing mice. Genes coding for pro-inflammatory or pro-apoptotic proteins are not overrepresented among differentially regulated genes. Even a decrease of inflammation markers is observed. This further supports the strategy to treat alzheimer’s disease by increasing the beta-secretase activity
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Anders, A.; Gilbert, S.; Garten, W.; Postina, R.; Fahrenholz, F.
Regulation of the alpha-secretase ADAM10 by its prodomain and proprotein convertases
FASEB J.
15
1837-1839
2001
Bos taurus, Homo sapiens
Manually annotated by BRENDA team
Janes, P.W.; Saha, N.; Barton, W.A.; Kolev, M.V.; Wimmer-Kleikamp, S.H.; Nievergall, E.; Blobel, C.P.; Himanen, J.P.; Lackmann, M.; Nikolov, D.B.
Adam meets Eph: an ADAM substrate recognition module acts as a molecular switch for ephrin cleavage in trans
Cell
123
291-304
2005
Bos taurus
Manually annotated by BRENDA team
Escrevente, C.; Morais, V.A.; Keller, S.; Soares, C.M.; Altevogt, P.; Costa, J.
Functional role of N-glycosylation from ADAM10 in processing, localization and activity of the enzyme
Biochim. Biophys. Acta
1780
905-913
2008
Bos taurus, Homo sapiens
Manually annotated by BRENDA team
Prinzen, C.; Truembach, D.; Wurst, W.; Endres, K.; Postina, R.; Fahrenholz, F.
Differential gene expression in ADAM10 and mutant ADAM10 transgenic mice
BMC Genomics
10
66
2009
Bos taurus
Manually annotated by BRENDA team