KEGG   ENZYME: 3.6.1.60
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
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)
R09881 R09882
Substrate
P1,P6-bis(5'-adenosyl)hexaphosphate [CPD:C20190];
H2O [CPD:C00001];
P1,P5-bis(5'-adenosyl)pentaphosphate [CPD:C04058]
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 3:20 (2002)
DOI:10.1186/1471-2091-3-20
  Sequence
[hsa:170685 55190]
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 274:21735-40 (1999)
DOI:10.1074/jbc.274.31.21735
  Sequence
[sce:YOR163W]
Other DBs
ExplorEnz - The Enzyme Database: 3.6.1.60
IUBMB Enzyme Nomenclature: 3.6.1.60
ExPASy - ENZYME nomenclature database: 3.6.1.60
BRENDA, the Enzyme Database: 3.6.1.60

  All links  
Chemical substance (6)   
   KEGG COMPOUND (6)   
Chemical reaction (3)   
   KEGG REACTION (2)   
   KEGG RCLASS (1)   
Protein sequence (26)   
   UniProt (13)   
   SWISS-PROT (6)   
   RefSeq(pep) (7)   
DNA sequence (15)   
   RefSeq(nuc) (8)   
   GenBank (3)   
   EMBL (4)   
Protein domain (5)   
   InterPro (5)   
All databases (55)   

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