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Information on EC 3.4.24.B8 - ADAM1 endopeptidase and Organism(s) Mus musculus and UniProt Accession Q60813

for references in articles please use BRENDA:EC3.4.24.B8
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.B8 ADAM1 endopeptidase
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This record set is specific for:
Mus musculus
UNIPROT: Q60813
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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
fertilin, fertilin alpha, ph-30, adam1a, adam1, adam1b, adam-1, adam 1, fertilin alpha subunit, a disintegrin and metalloprotease 1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
a disintegrin and metalloproteinase domain 1a
-
fertilin alpha 1a subunit
-
a disintegrin and metalloprotease 1
-
-
a disintegrin and metalloproteinase domain 1b
-
ADAM1
-
-
ADAM1a
-
-
ADAM1b
-
-
fertilin
-
-
fertilin alpha
-
heterodimeric protein consisting of ADAM1 and ADAM2 located on the surface of sperm
fertilin alpha 1b subunit
-
M12.201
PH-30
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
proteolytic degradation of proteins
show the reaction diagram
mechanism
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
CAS REGISTRY NUMBER
COMMENTARY hide
252337-44-3
-
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
-
-
?
proteins + H2O
peptides
show the reaction diagram
additional information
?
-
-
the enzyme mediates the cell-cell membrane fusion of egg and sperm
-
?
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
-
-
?
proteins + H2O
peptides
show the reaction diagram
additional information
?
-
-
the enzyme mediates the cell-cell membrane fusion of egg and sperm
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
activates, required
Mg2+
-
activates
Mn2+
-
activates
additional information
-
divalent cations are required for membrane fusion
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
binding to the egg is reduced by treatment with chymotrypsin
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
precursor
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
isozyme a
Manually annotated by BRENDA team
-
2 isozymes
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ADM1A_MOUSE
791
0
87490
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100000
-
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
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
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
60000
-
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
SUBUNIT
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
dimer
-
-
additional information
-
the alpha subunit contains a putative fusion peptide, beta subunit contains a soluble disintegrin ligand
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
-
N-glycosylation
proteolytic modification
-
isozyme a is partially processed to a 48 kDa mature protein in round and elongating spermatids, isozyme b precursor is totally processed to a 63 kDa intermediate during spermatogenesis and finally to a 60 kDa mature protein during sperm transit in the epididymis
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of subunit alpha as fusion protein with maltose binding protein in Escherichia coli DH5alpha
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
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
Mus musculus (Q60813), Mus musculus (Q8R534), Rattus norvegicus (P70505)
Manually annotated by BRENDA team
Kim, E.; Nishimura, H.; Baba, T.
Differential localization of ADAM1a and ADAM1b in the endoplasmic reticulum of testicular germ cells and on the surface of epididymal sperm
Biochem. Biophys. Res. Commun.
304
313-319
2003
Mus musculus
Manually annotated by BRENDA team
Evans, J.P.; Schultz, R.M.; Kopf, G.S.
Characterization of the binding of recombinant mouse sperm fertilin alpha subunit to mouse eggs: evidence for function as a cell adhesion molecule in sperm-egg binding
Dev. Biol.
187
94-106
1997
Mus musculus
Manually annotated by BRENDA team
Nishimura, H.; Kim, E.; Nakanishi, T.; Baba, T.
Possible function of the ADAM1a/ADAM2 Fertilin complex in the appearance of ADAM3 on the sperm surface
J. Biol. Chem.
279
34957-34962
2004
Mus musculus
Manually annotated by BRENDA team
Kim, E.; Yamashita, M.; Nakanishi, T.; Park, K.E.; Kimura, M.; Kashiwabara, S.; Baba, T.
Mouse sperm lacking ADAM1b/ADAM2 fertilin can fuse with the egg plasma membrane and effect fertilization
J. Biol. Chem.
281
5634-5639
2006
Mus musculus
Manually annotated by BRENDA team