KEGG   ENZYME: 3.6.1.52Help
Entry
EC 3.6.1.52                 Enzyme                                 

Name
diphosphoinositol-polyphosphate diphosphatase;
diphosphoinositol-polyphosphate phosphohydrolase;
DIPP
Class
Hydrolases;
Acting on acid anhydrides;
In phosphorus-containing anhydrides
BRITE hierarchy
Sysname
diphospho-myo-inositol-polyphosphate diphosphohydrolase
Reaction(IUBMB)
diphospho-myo-inositol polyphosphate + H2O = myo-inositol polyphosphate + phosphate [RN:R05777]
Reaction(KEGG)
Substrate
diphospho-myo-inositol polyphosphate [CPD:C11524];
H2O [CPD:C00001]
Product
myo-inositol polyphosphate [CPD:C11525];
phosphate [CPD:C00009]
Comment
This enzyme hydrolyses the diphosphate bond, leaving a phospho group where a diphospho group had been. It can also act on bis(adenosine) diphosphate.
History
EC 3.6.1.52 created 2002
Orthology
K07766  
diphosphoinositol-polyphosphate diphosphatase
Genes
HSA: 
11163(NUDT4) 11165(NUDT3) 170685(NUDT10) 55190(NUDT11)
PTR: 
465637(NUDT11) 736394(NUDT4)
PPS: 
GGO: 
PON: 
NLE: 
100583670(NUDT10) 100584216(NUDT11) 100602253(NUDT4)
MCC: 
695921 695959 715385(NUDT4) 718568(NUDT3)
MCF: 
101867035 102136605(NUDT10) 102137860(NUDT11) 102140245(NUDT3)
CJC: 
MMU: 
102954(Nudt10) 56409(Nudt3) 58242(Nudt11) 71207(Nudt4)
RNO: 
294292(Nudt3) 367747(Nudt10) 680248(Nudt11) 94267(Nudt4)
CGE: 
HGL: 
TUP: 
CFA: 
100846983(NUDT3) 475425(NUDT4) 491890(NUDT10) 612593(NUDT10)
AML: 
UMR: 
FCA: 
PTG: 
BTA: 
614183(NUDT4) 616931(NUDT10) 618855(NUDT3) 785611(NUDT11)
BOM: 
PHD: 
102344185(NUDT4)
CHX: 
OAS: 
SSC: 
CFR: 
BACU: 
LVE: 
ECB: 
100064437(NUDT4) 102149351(NUDT3)
MYB: 
MYD: 
102757376(NUDT3) 102766076(NUDT4) 102769935(NUDT10)
PALE: 
MDO: 
100015435(NUDT4) 103106377(NUDT3)
SHR: 
OAA: 
100073927(NUDT4) 100088959(NUDT3)
GGA: 
417897(NUDT4) 419905(NUDT3)
MGP: 
APLA: 
101805371(NUDT4)
TGU: 
FAB: 
101815641(NUDT4)
PHI: 
102110920(NUDT3) 102113614(NUDT4)
FPG: 
101910592(NUDT3) 101915353(NUDT4)
FCH: 
102046910(NUDT4)
CLV: 
102096810(NUDT4) 102097363(NUDT3)
ASN: 
102368135(NUDT4) 102381897(NUDT3)
AMJ: 
102566648(NUDT3) 102573038(NUDT4)
PSS: 
CMY: 
102938043(NUDT3) 102946204(NUDT4)
ACS: 
100560847(nudt4)
PBI: 
XLA: 
447697 495434(nudt4)
XTR: 
448180(nudt4)
DRE: 
378990(nudt4a) 394120(nudt3a) 447910(nudt4b) 450013(nudt3b)
TRU: 
MZE: 
OLA: 
XMA: 
LCM: 
102357558(NUDT4) 102363264(NUDT3)
CMK: 
BFO: 
CIN: 
SPU: 
DME: 
DPO: 
DAN: 
DER: 
DPE: 
DSE: 
DSI: 
DWI: 
DYA: 
DGR: 
DMO: 
DVI: 
AGA: 
AAG: 
CQU: 
AME: 
409489(Aps)
NVI: 
TCA: 
BMOR: 
API: 
PHU: 
ISC: 
CEL: 
CELE_R119.3(R119.3) CELE_Y92H12BL.5(Y92H12BL.5)
CBR: 
BMY: 
LOA: 
TSP: 
HRO: 
LGI: 
NVE: 
TAD: 
AQU: 
ATH: 
AT1G73540(NUDT21)
ALY: 
CRB: 
EUS: 
TCC: 
GMX: 
PVU: 
MTR: 
CAM: 
FVE: 
PPER: 
PMUM: 
MDM: 
CSV: 
CMO: 
RCU: 
POP: 
POPTR_0015s04970g(POPTRDRAFT_575041)
VVI: 
SLY: 
SOT: 
OSA: 
DOSA: 
Os06t0255400-01(Os06g0255400)
OBR: 
BDI: 
SBI: 
SORBI_06g014790(SORBIDRAFT_06g014790) SORBI_10g009220(SORBIDRAFT_10g009220)
ZMA: 
SITA: 
PDA: 
SMO: 
PPP: 
CRE: 
VCN: 
OLU: 
MPP: 
CVR: 
CME: 
GSL: 
SCE: 
YOR163W(DDP1)
AGO: 
ERC: 
KLA: 
LTH: 
VPO: 
ZRO: 
CGR: 
NCS: 
NCAS_0F00300(NCAS0F00300)
NDI: 
NDAI_0K02830(NDAI0K02830)
TPF: 
TPHA_0J00610(TPHA0J00610)
TBL: 
TBLA_0E03250(TBLA0E03250)
TDL: 
TDEL_0G04120(TDEL0G04120)
KAF: 
KAFR_0G02550(KAFR0G02550)
PPA: 
DHA: 
PIC: 
PGU: 
SPAA: 
LEL: 
CAL: 
CTP: 
COT: 
CDU: 
CTEN: 
YLI: 
CLU: 
NCR: 
SMP: 
PAN: 
TTT: 
MTM: 
CTHR: 
MGR: 
TMN: 
FGR: 
NHE: 
TRE: 
MAW: 
MAJ: 
CMT: 
VAL: 
ELA: 
SSL: 
BFU: 
MBE: 
ANI: 
AFM: 
AOR: 
AOR_1_616014(AO090026000332)
ANG: 
ANI_1_244024(An02g01790)
AFV: 
ACT: 
NFI: 
PCS: 
CIM: 
CPW: 
PBL: 
URE: 
TVE: 
AJE: 
PNO: 
PTE: 
BZE: 
BSC: 
BOR: 
ZTR: 
PFJ: 
BCOM: 
NPA: 
TML: 
SPO: 
TMS: 
ADL: 
FME: 
CCI: 
SCM: 
CPUT: 
SLA: 
UMA: 
MGL: 
PGR: 
MLR: 
WSE: 
MBR: 
PTI: 
TPS: 
PIF: 
GTT: 
 » show all
Taxonomy
Reference
1  [PMID:9822604]
  Authors
Safrany ST, Caffrey JJ, Yang X, Bembenek ME, Moyer MB, Burkhart WA, Shears SB.
  Title
A novel context for the 'MutT' module, a guardian of cell integrity, in a diphosphoinositol polyphosphate phosphohydrolase.
  Journal
EMBO. J. 17 (1998) 6599-607.
  Sequence
[hsa:11165]
Reference
2  [PMID:10777568]
  Authors
Caffrey JJ, Safrany ST, Yang X, Shears SB.
  Title
Discovery of molecular and catalytic diversity among human diphosphoinositol-polyphosphate phosphohydrolases. An expanding Nudt family.
  Journal
J. Biol. Chem. 275 (2000) 12730-6.
  Sequence
[hsa:11163]
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 

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 [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 (2002) 20.
  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.
  Sequence
[up:Q09790]
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 

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