KEGG   ENZYME: 3.6.1.60Help
Entry
EC 3.6.1.60                 Enzyme                                 

Name
diadenosine hexaphosphate hydrolase (AMP-forming);
hAps1;
NUDT11 (gene name);
hAps2;
NUDT10 (gene name)
Class
Hydrolases;
Acting on acid anhydrides;
In phosphorus-containing anhydrides
BRITE hierarchy
Sysname
P1,P6-bis(5'-adenosyl)hexaphosphate nucleotidohydrolase (AMP-forming)
Reaction(IUBMB)
(1) P1,P6-bis(5'-adenosyl)hexaphosphate + H2O = adenosine 5'-pentaphosphate + AMP [RN:R09881];
(2) P1,P5-bis(5'-adenosyl)pentaphosphate + H2O = adenosine 5'-tetraphosphate + AMP [RN:R09882]
Reaction(KEGG)
Substrate
P1,P6-bis(5'-adenosyl)hexaphosphate [CPD:C20190];
H2O [CPD:C00001];
P1,P5-bis(5'-adenosyl)pentaphosphate
Product
adenosine 5'-pentaphosphate [CPD:C20198];
AMP [CPD:C00020];
adenosine 5'-tetraphosphate [CPD:C03483]
Comment
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.
History
EC 3.6.1.60 created 2012
Reference
1  [PMID:12121577]
  Authors
Leslie NR, McLennan AG, Safrany ST
  Title
Cloning and characterisation of hAps1 and hAps2, human diadenosine polyphosphate-metabolising Nudix hydrolases.
  Journal
BMC. Biochem. 3 (2002) 20.
  Organism
Homo sapiens
  Sequence
Reference
2  [PMID:10419486]
  Authors
Safrany ST, Ingram SW, Cartwright JL, Falck JR, McLennan AG, Barnes LD, Shears SB
  Title
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.
  Journal
J. Biol. Chem. 274 (1999) 21735-40.
  Organism
Schizosaccharomyces pombe, Saccharomyces cerevisiae
  Sequence
[up:Q09790]
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 

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