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Information on EC 3.6.1.5 - apyrase and Organism(s) Aedes albopictus and UniProt Accession E0D877

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EC Tree
     3 Hydrolases
         3.6 Acting on acid anhydrides
             3.6.1 In phosphorus-containing anhydrides
                3.6.1.5 apyrase
IUBMB Comments
Apyrases are active against both di- and triphosphate nucleotides (NDPs and NTPs) and hydrolyse NTPs to nucleotide monophosphates (NMPs) in two distinct successive phosphate-releasing steps, with NDPs as intermediates. They differ from ATPases, which specifically hydrolyse ATP, by hydrolysing both ATP and ADP. The eukaryotic enzymes requires Ca2+, but Mg2+ can substitute. Most of the ecto-ATPases that occur on the cell surface and hydrolyse extracellular nucleotides belong to this enzyme family.
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This record set is specific for:
Aedes albopictus
UNIPROT: E0D877
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Word Map
The taxonomic range for the selected organisms is: Aedes albopictus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
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Synonyms
apyrase, ecto-atpase, adpase, ntpdase3, atp diphosphohydrolase, entpd1, atpase 2, ecto-apyrase, ectonucleoside triphosphate diphosphohydrolase, atpdase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ATP diphosphohydrolase
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adenosine diphosphatase
-
-
-
-
ADPase
-
-
-
-
ATP-diphosphatase
-
-
-
-
ATP-diphosphohydrolase
-
-
-
-
ATPDase
-
-
-
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CD39 antigen
-
-
-
-
Golgi nucleoside diphosphatase
-
-
-
-
HB6
-
-
-
-
Lymphoid cell activation antigen
-
-
-
-
NTPDase1
-
-
-
-
NTPDase3
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphorous acid anhydride hydrolysis
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-
-
-
SYSTEMATIC NAME
IUBMB Comments
nucleoside triphosphate phosphohydrolase (nucleoside monophosphoate-forming)
Apyrases are active against both di- and triphosphate nucleotides (NDPs and NTPs) and hydrolyse NTPs to nucleotide monophosphates (NMPs) in two distinct successive phosphate-releasing steps, with NDPs as intermediates. They differ from ATPases, which specifically hydrolyse ATP, by hydrolysing both ATP and ADP. The eukaryotic enzymes requires Ca2+, but Mg2+ can substitute. Most of the ecto-ATPases that occur on the cell surface and hydrolyse extracellular nucleotides belong to this enzyme family.
CAS REGISTRY NUMBER
COMMENTARY hide
9000-95-7
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
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-
-
?
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
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
-
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
apyrases can inhibit platelet activation by depletion of adenosine diphosphate
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
APY_AEDAL
564
1
62751
Swiss-Prot
Secretory Pathway (Reliability: 1)
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography, denaturing by urea and renaturing using glutathione and dialysis
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of His-tagged enzyme in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Dong, F.; Fu, Y.; Li, X.; Jiang, J.; Sun, J.; Cheng, X.
Cloning, expression, and characterization of salivary apyrase from Aedes albopictus
Parasitol. Res.
110
931-937
2012
Aedes albopictus (E0D877), Aedes albopictus
Manually annotated by BRENDA team