Information on EC 3.4.24.B8 - ADAM1 endopeptidase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.4.24.B8
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
ADAM1 endopeptidase
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
proteolytic degradation of proteins
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
CAS REGISTRY NUMBER
COMMENTARY hide
252337-44-3
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
precursor
SwissProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
-
ADAM-1 forms a fertilin complex involved in key steps of the sperm-oocyte membrane interaction
SUBSTRATE
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
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
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
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
activates, required
Mg2+
-
activates
Mn2+
-
activates
Zn2+
metalloprotease domain in the beta subunit precursor region, but not in the mature protein, the alpha-subunit conatins a metalloprotease domain, which is the active site, in the mature from with the consensus sequence HEXXHXXGXXHE
additional information
-
divalent cations are required for membrane fusion
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
binding to the egg is reduced by treatment with chymotrypsin
-
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
isozyme a
Manually annotated by BRENDA team
additional information
-
isozymes precursors form in each case a heterodimer with ADAM2
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10800
-
estimated from SDS-PAGE band pattern
44000
-
1 * 60000, alpha subunit, + 1 * 44000, beta subunit, SDS-PAGE
48000
-
x * 48000, mature isozyme a, SDS-PAGE, x * 60000, mature isozyme b, SDS-PAGE, x * 100000, precursor of isozyme a, SDS-PAGE, x * 120000, precursor of isozyme b, SDS-PAGE
95000
-
unprocessed expected mass of ADAM-1
100000
120000
-
x * 48000, mature isozyme a, SDS-PAGE, x * 60000, mature isozyme b, SDS-PAGE, x * 100000, precursor of isozyme a, SDS-PAGE, x * 120000, precursor of isozyme b, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 48000, mature isozyme a, SDS-PAGE, x * 60000, mature isozyme b, SDS-PAGE, x * 100000, precursor of isozyme a, SDS-PAGE, x * 120000, precursor of isozyme b, SDS-PAGE
homodimer
-
x * 50000-55000, SDS-PAGE
homotrimer
-
3 * 3600, estimated from SDS-PAGE band pattern
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
proteolytic modification
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination, alpha and beta subunits
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expression of subunit alpha as fusion protein with maltose binding protein in Escherichia coli DH5alpha
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine