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Information on EC 3.6.1.60 - diadenosine hexaphosphate hydrolase (AMP-forming) and Organism(s) Homo sapiens and UniProt Accession O95989
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3.6.1.60 diadenosine hexaphosphate hydrolase (AMP-forming)IUBMB 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.
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Word Map
- 3.6.1.60
- polyphosphates
-
diphosphoinositol
- prostate
- autoantibody
-
nudix
-
serous
-
nappa
-
tumor-associated
- dipps
-
phosphohydrolases
- trim39
- medicine
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
nudt10, nudt11, haps1, haps2, atnudt13, at3g26690, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
P1,P6-bis(5'-adenosyl)hexaphosphate + H2O = adenosine 5'-pentaphosphate + AMP
(1)
P1,P5-bis(5'-adenosyl)pentaphosphate + H2O = adenosine 5'-tetraphosphate + AMP
(2)
SYSTEMATIC NAME
IUBMB Comments
P1,P6-bis(5'-adenosyl)hexaphosphate nucleotidohydrolase (AMP-forming)
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.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
P1,P5-bis(5'-adenosyl)pentaphosphate + H2O
adenosine 5'-tetraphosphate + AMP
the enzyme degrades P1,P6-bis(5'-adenosyl)hexaphosphate and P1,P5-bis(5'-adenosyl)pentaphosphate, in preference to other diadenosine polyphosphates
-
-
?
P1,P6-bis(5'-adenosyl)hexaphosphate + H2O
adenosine 5'-pentaphosphate + AMP
the predominant route of P1,P6-bis(5'-adenosyl)hexaphosphate hydrolysis is to AMP plus P1,P5-bis(5'-adenosyl)pentaphosphate, with the formation of ADP plus p4A being a more minor reaction. The enzyme degrades P1,P6-bis(5'-adenosyl)hexaphosphate and P1,P5-bis(5'-adenosyl)pentaphosphate, in preference to other diadenosine polyphosphates
-
-
?
P1,P4-bis(5'-adenosyl)tetraphosphate + H2O
ATP + AMP
weak activity
-
-
?
additional information
?
-
the enzyme also catalyses the hydrolysis of diphosphoinositol pentakisphosphate
-
-
?
P1,P5-bis(5'-adenosyl)pentaphosphate + H2O
adenosine 5'-tetraphosphate + AMP
marked preference for adenine over guanine nucleotides. The enzyme controls intracellular P1,P5-bis(5'-adenosyl)pentaphosphate and P1,P6-bis(5'-adenosyl)hexaphosphate levels
-
-
?
P1,P5-bis(5'-adenosyl)pentaphosphate + H2O
adenosine 5'-tetraphosphate + AMP
marked preference for adenine over guanine nucleotides. The most rapidly metabolised substrate appears to be P1,P5-bis(5'-adenosyl)pentaphosphate, although P1,P6-bis(5'-adenosyl)hexaphosphate is bound with higher affinity
-
-
?
P1,P6-bis(5'-adenosyl)hexaphosphate + H2O
adenosine 5'-pentaphosphate + AMP
marked preference for adenine over guanine nucleotides. The enzyme controls intracellular P1,P5-bis(5'-adenosyl)pentaphosphate and P1,P6-bis(5'-adenosyl)hexaphosphate levels
-
-
?
P1,P6-bis(5'-adenosyl)hexaphosphate + H2O
adenosine 5'-pentaphosphate + AMP
marked preference for adenine over guanine nucleotides. The most rapidly metabolised substrate appears to be P1,P5-bis(5'-adenosyl)pentaphosphate, although P1,P6-bis(5'-adenosyl)hexaphosphate is bound with higher affinity
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
P1,P5-bis(5'-adenosyl)pentaphosphate + H2O
adenosine 5'-tetraphosphate + AMP
marked preference for adenine over guanine nucleotides. The enzyme controls intracellular P1,P5-bis(5'-adenosyl)pentaphosphate and P1,P6-bis(5'-adenosyl)hexaphosphate levels
-
-
?
P1,P6-bis(5'-adenosyl)hexaphosphate + H2O
adenosine 5'-pentaphosphate + AMP
marked preference for adenine over guanine nucleotides. The enzyme controls intracellular P1,P5-bis(5'-adenosyl)pentaphosphate and P1,P6-bis(5'-adenosyl)hexaphosphate levels
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
a divalent cation is essential for activity, with Mn2+ by far the most effective between 2 and 6 mM. Cu2+ supports less than 30% and Zn2+ and Co2+ each less than 3% of the maximum activity
Cu2+
a divalent cation is essential for activity, with Mn2+ by far the most effective between 2 and 6 mM. Cu2+ supports less than 30% and Zn2+ and Co2+ each less than 3% of the maximum activity
Mn2+
a divalent cation is essential for activity, with Mn2+ by far the most effective between 2 and 6 mM. Cu2+ supports less than 30% and Zn2+ and Co2+ each less than 3% of the maximum activity
Zn2+
a divalent cation is essential for activity, with Mn2+ by far the most effective between 2 and 6 mM. Cu2+ supports less than 30% and Zn2+ and Co2+ each less than 3% of the maximum activity
additional information
additional information
Mg2+, Ni2+ and Ca1+ are not able to activate the enzyme
additional information
Mg2+, Ni2+ and Ca1+ are not able to activate the enzyme
additional information
-
Mg2+, Ni2+ and Ca1+ are not able to activate the enzyme
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.011
P1,P5-bis(5'-adenosyl)pentaphosphate
pH 7.6, 37°C, hApsI-39N
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5 - 9
7.5 - 9
pH 7.5: about 55% of maximal activity, pH 8.5-9: maximal activity
7.5 - 9
pH 7.5: about 60% of maximal activity, pH 9: about 90% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
no signal for hAps1 is detected in placenta, liver, skeletal muscle, kidney, spleen, colon or peripheral blood leukocytes. No activity in breast GI-101 cells, lung LX-1 cells, colon CX-1 cells, lung GI-117 cells, colon GI-112 cells and pancreas GI-103 cells
additional information
no signal for hAps1 is detected in placenta, liver, skeletal muscle, kidney, spleen, colon or peripheral blood leukocytes. No activity in breast GI-101 cells, lung LX-1 cells, colon CX-1 cells, lung GI-117 cells, colon GI-112 cells and pancreas GI-103 cells
additional information
-
no signal for hAps1 is detected in placenta, liver, skeletal muscle, kidney, spleen, colon or peripheral blood leukocytes. No activity in breast GI-101 cells, lung LX-1 cells, colon CX-1 cells, lung GI-117 cells, colon GI-112 cells and pancreas GI-103 cells
additional information
no signal for hAps2 is found in skeletal muscle, thymus, small intestine, colon or peripheral blood leukocytes. No activity in tumour cell lines from breast GI-101, lung LX-1, colon CX-1, lung GI-117, colon GI-112 and pancreas GI-103
additional information
no signal for hAps2 is found in skeletal muscle, thymus, small intestine, colon or peripheral blood leukocytes. No activity in tumour cell lines from breast GI-101, lung LX-1, colon CX-1, lung GI-117, colon GI-112 and pancreas GI-103
additional information
-
no signal for hAps2 is found in skeletal muscle, thymus, small intestine, colon or peripheral blood leukocytes. No activity in tumour cell lines from breast GI-101, lung LX-1, colon CX-1, lung GI-117, colon GI-112 and pancreas GI-103
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
suppressing the expression of NUDT11, SLC22A3, and HNF1B influences cellular phenotypes associated with tumor-related properties in prostate cancer cells. 4 of the 12 known risk polymorphisms are strongly associated with transcripts NUDT11, MSMB, NCOA4, SLC22A3, and HNF1B in histologically normal tissue. Although associations are also observed in tumor tissue, they tend to be more attenuated
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Safrany, S.T.; Ingram, S.W.; Cartwright, J.L.; Falck, J.R.; McLennan, A.G.; Barnes, L.D.; 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
21735-21740
1999
Homo sapiens (O95989)
Leslie, N.R.; McLennan, A.G.; Safrany, S.T.
Cloning and characterisation of hAps1 and hAps2, human diadenosine polyphosphate-metabolising Nudix hydrolases
BMC Biochem.
3
20
2002
Homo sapiens (Q8NFP7), Homo sapiens (Q96G61), Homo sapiens
Grisanzio, C.; Werner, L.; Takeda, D.; Awoyemi, B.C.; Pomerantz, M.M.; Yamada, H.; Sooriakumaran, P.; Robinson, B.D.; Leung, R.; Schinzel, A.C.; Mills, I.; Ross-Adams, H.; Neal, D.E.; Kido, M.; Yamamoto, T.; Petrozziello, G.; Stack, E.C.; Lis, R.; Kantoff, P.W.; Loda, M.; Sartor, O.; Egawa, S.; Tewari, A.K.
Genetic and functional analyses implicate the NUDT11, HNF1B, and SLC22A3 genes in prostate cancer pathogenesis
Proc. Natl. Acad. Sci. USA
109
11252-11257
2012
Homo sapiens (Q96G61), Homo sapiens
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