EC 3.6.1.5 - Apyrase

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IntEnz Enzyme Nomenclature
EC 3.6.1.5

Names

Accepted name:
apyrase
Other names:
ADPase
ATP diphosphohydrolase [ambiguous]
ATP-diphosphatase
adenosine diphosphatase
ATP-diphosphohydrolase
Systematic name:
nucleoside triphosphate phosphohydrolase (nucleoside monophosphoate-forming)

Reactions

Cofactor

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.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Protein domains and families: PROSITE:PDOC00952
Structural data: CSA , EC2PDB
Gene Ontology: GO:0102490 , GO:0102489 , GO:0102485 , GO:0102486 , GO:0102491 , GO:0102488 , GO:0102487
CAS Registry Number: 9000-95-7
UniProtKB/Swiss-Prot: (28) [show] [UniProt]

References

  1. Krishman, P.S.
    Apyrase, pyrophosphatase and metaphosphatase of Penicillium chrysogenum.
    Arch. Biochem. Biophys. 37: 224-234 (1952). [PMID: 14953432]
  2. Liébecq, C., Lallemand, A. and Degueldre-Guillaume, M.-J.
    [Partial purification and properties of potato apyrase.]
    Bull. Soc. Chim. Biol. 45: 573-594 (1963). [PMID: 13930517]
  3. Chen, Y. R., Datta, N., Roux, S. J.
    Purification and partial characterization of a calmodulin-stimulated nucleoside triphosphatase from pea nuclei.
    J. Biol. Chem. 262: 10689-10694 (1987). [PMID: 3038893]
  4. Christoforidis, S., Papamarcaki, T., Galaris, D., Kellner, R., Tsolas, O.
    Purification and properties of human placental ATP diphosphohydrolase.
    Eur. J. Biochem. 234: 66-74 (1995). [PMID: 8529670]
  5. Wang, T. F., Guidotti, G.
    CD39 is an ecto-(Ca2+,Mg2+)-apyrase.
    J. Biol. Chem. 271: 9898-9901 (1996). [PMID: 8626624]
  6. Gao, X. D., Kaigorodov, V., Jigami, Y.
    YND1, a homologue of GDA1, encodes membrane-bound apyrase required for Golgi N- and O-glycosylation in Saccharomyces cerevisiae.
    J. Biol. Chem. 274: 21450-21456 (1999). [PMID: 10409709]
  7. Xu, W., Jones, C. R., Dunn, C. A., Bessman, M. J.
    Gene ytkD of Bacillus subtilis encodes an atypical nucleoside triphosphatase member of the Nudix hydrolase superfamily.
    J. Bacteriol. 186: 8380-8384 (2004). [PMID: 15576788]

[EC 3.6.1.5 created 1961, modified 1976, modified 2000, modified 2013]