ExplorEnz: EC 3.6.1.60

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3.6.1.60

Accepted name:

diadenosine hexaphosphate hydrolase (AMP-forming)

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

Other name(s):

hAps1; NUDT11 (gene name); hAps2; NUDT10 (gene name)

Systematic name:

P¹,P⁶-bis(5′-adenosyl)hexaphosphate nucleotidohydrolase (AMP-forming)

Comments:

A divalent cation is essential for activity. Mn²⁺ (2–6 mM) is most effective. The enzyme controls intracellular levels of P¹,P⁵-bis(5′-adenosyl)pentaphosphate and P1,P6-bis(5′-adenosyl)hexaphosphate. Weak activity with P1,P4-bis(5′-adenosyl)tetraphosphate. Marked preference for adenine over guanine nucleotides.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB

References:

Leslie, N.R., McLennan, A.G. and Safrany, S.T. Cloning and characterisation of hAps1 and hAps2, human diadenosine polyphosphate-metabolising Nudix hydrolases. BMC Biochem. 3:20 (2002). [DOI] [PMID: 12121577]

Safrany, S.T., Ingram, S.W., Cartwright, J.L., Falck, J.R., McLennan, A.G., Barnes, L.D. and Shears, S.B. 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 (1999) 21735–21740. [DOI] [PMID: 10419486]

[EC 3.6.1.60 created 2012]