Diadenosine hexaphosphate hydrolase (AMP-forming)

Diadenosine hexaphosphate hydrolase (AMP-forming)
Identifiers
EC number 3.6.1.60
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

Diadenosine hexaphosphate hydrolase (AMP-forming) (EC 3.6.1.60, hAps1, NUDT11 (gene), hAps2, NUDT10 (gene)) is an enzyme with systematic name P1,P6-bis(5'-adenosyl)hexaphosphate nucleotidohydrolase (AMP-forming).[1][2] This enzyme catalyses the following chemical reaction

(1) P1,P6-bis(5'-adenosyl)hexaphosphate + H2O adenosine 5'-pentaphosphate + AMP
(2) P1,P5-bis(5'-adenosyl)pentaphosphate + H2O adenosine 5'-tetraphosphate + AMP

A divalent cation is essential for activity.

References

  1. Leslie, N.R.; McLennan, A.G.; Safrany, S.T. (2002). "Cloning and characterisation of hAps1 and hAps2, human diadenosine polyphosphate-metabolising Nudix hydrolases". BMC Biochem. 3: #20–20. doi:10.1186/1471-2091-3-20. PMC 117780Freely accessible. PMID 12121577.
  2. Safrany, S.T.; Ingram, S.W.; Cartwright, J.L.; Falck, J.R.; McLennan, A.G.; Barnes, L.D.; Shears, S.B. (1999). "The diadenosine hexaphosphate hydrolases from Schizosaccharomyces pombe and Saccharomyces cerevisiae are homologues of the human diphosphoinositol polyphosphate phosphohydrolase. Overlapping substrate specificities in a MutT-type protein". J. Biol. Chem. 274: 21735–21740. doi:10.1074/jbc.274.31.21735. PMID 10419486.

External links

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