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Information on EC 3.6.1.14 - adenosine-tetraphosphatase
for references in articles please use BRENDA:EC3.6.1.14
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EC Tree 3 Hydrolases
3.6 Acting on acid anhydrides
3.6.1 In phosphorus-containing anhydrides
3.6.1.14 adenosine-tetraphosphatase
IUBMB Comments
Also acts on inosine tetraphosphate and tripolyphosphate but shows little or no activity with other nucleotides or polyphosphates.
The enzyme appears in viruses and cellular organisms
- 3.6.1.14
-
lupin
- 5'-tetraphosphate
- yellow
- p5a
- orthophosphate
-
3.6.1.17
- 5'-pentaphosphate
-
tetraphosphatases
- guanosine
showSynonyms
adenosinetetraphosphatase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
adenosinetetraphosphatase
-
-
-
-
nucleoside tetraphosphatase
p4A phosphohydrolase
-
-
-
-
phosphatase, adenosine tetra-
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
adenosine 5'-tetraphosphate + H2O = ATP + phosphate
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphorous acid anhydride hydrolysis
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
KEGG
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SYSTEMATIC NAME
IUBMB Comments
adenosine-tetraphosphate phosphohydrolase
Also acts on inosine tetraphosphate and tripolyphosphate but shows little or no activity with other nucleotides or polyphosphates.
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CAS REGISTRY NUMBER
COMMENTARY
37289-26-2
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
alpha-beta-methylene-adenosine 5'-tetraphosphate + H2O
alpha-beta-methylene-adenosine 5'-triphosphate + phosphate
ATP + phosphate
adenosine 5'-tetraphosphate + H2O
-
Substrates: enzyme nicotinate phosphoribosyltransferase, EC 6.3.4.21, is able to generate adenosine 5'-tetraphosphate using substrate ATP and product phosphate. Accompanying a typically irreversible hydrolysis of ATP to ADP and phosphate, is a fully reversible phosphate transfer reaction between ATP and adenosine 5'-tetraphosphate
Products: -
Products: -
?
adenosine 5'-pentaphosphate + H2O
?
-
Substrates: hydrolyzed 18fold more slowly than adenosine 5'-tetraphosphate
Products: -
Products: -
?
adenosine 5'-pentaphosphate + H2O
?
-
Substrates: hydrolyzed at 1/200 the rate of adenosine 5'-tetraphosphate
Products: -
Products: -
?
adenosine 5'-tetraphosphate + H2O
ATP + phosphate
-
Substrates: -
Products: -
Products: -
?
adenosine 5'-tetraphosphate + H2O
ATP + phosphate
-
Substrates: -
Products: -
Products: -
?
adenosine 5'-tetraphosphate + H2O
ATP + phosphate
-
Substrates: -
Products: -
Products: -
?
alpha-beta-methylene-adenosine 5'-tetraphosphate + H2O
alpha-beta-methylene-adenosine 5'-triphosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
alpha-beta-methylene-adenosine 5'-tetraphosphate + H2O
alpha-beta-methylene-adenosine 5'-triphosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
guanosine tetraphosphate + H2O
GTP + phosphate
-
Substrates: -
Products: -
Products: -
?
inosine tetraphosphate + H2O
ITP + phosphate
-
Substrates: -
Products: -
Products: -
?
inosine tetraphosphate + H2O
ITP + phosphate
-
Substrates: -
Products: -
Products: -
?
tripolyphosphate + H2O
diphosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
Fe2+
-
divalent metal ion required, the order of decreasing effectiveness for hydrolysis of adenosine 5'-tetraphosphate is: Co2+, Fe2+, Mg2+, Ni2+, Mn2+. For tripolyphosphate hydrolysis the order is: Ni2+, Co2+, Fe2+, Mg2+, Mn2+
Mg2+
Mn2+
Ni2+
Co2+
-
divalent metal ion required, the order of decreasing effectiveness for hydrolysis of adenosine 5'-tetraphosphate is: Co2+, Fe2+, Mg2+, Ni2+, Mn2+. For tripolyphosphate hydrolysis the order is: Ni2+, Co2+, Fe2+, Mg2+, Mn2+
Co2+
-
divalent cations activate hydrolysis of adenosine 5'-tetraphosphate in the order of decreasing effectiveness: Co2+, Mn2+, Mg2+, Ni2+
Mg2+
-
divalent metal ion required, the order of decreasing effectiveness for hydrolysis of adenosine tetraphosphate is: Co2+, Fe2+, Mg2+, Ni2+, Mn2+. For tripolyphosphate hydrolysis the order is: Ni2+, Co2+, Fe2+, Mg2+, Mn2+
Mg2+
-
divalent cations activate hydrolysis of adenosine 5'-tetraphosphate in the order of decreasing effectiveness: Co2+, Mn2+, Mg2+, Ni2+
Mn2+
-
divalent metal ion required, the order of decreasing effectiveness for hydrolysis of adenosine tetraphosphate is: Co2+, Fe2+, Mg2+, Ni2+, Mn2+. For tripolyphosphate hydrolysis the order is: Ni2+, Co2+, Fe2+, Mg2+, Mn2+
Mn2+
-
divalent cations activate hydrolysis of adenosine 5'-tetraphosphate in the order of decreasing effectiveness: Co2+, Mn2+, Mg2+, Ni2+
Ni2+
-
divalent metal ion required, the order of decreasing effectiveness for hydrolysis of adenosine tetraphosphate is: Co2+, Fe2+, Mg2+, Ni2+, Mn2+. For tripolyphosphate hydrolysis the order is: Ni2+, Co2+, Fe2+, Mg2+, Mn2+
Ni2+
-
divalent cations activate hydrolysis of adenosine 5'-tetraphosphate in the order of decreasing effectiveness: Co2+, Mn2+, Mg2+, Ni2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
no inhibition by alphabeta-methylene-adenosine 5'-tetraphosphate, betagamma-methylene adenosine 5'-tetraphosphate, gammadelta-methylene 5'-tetraphosphate, alphabeta-gammadelta-bismethylene-adenosine 5'-tetraphosphate, alphabeta-betagamma-bismethylene-adenosine 5'-tetraphosphate, and betagamma-gammadelta-bis(dichloro)methylene-adenosine 5'-tetraphosphate
-
additional information
-
no inhibition by alphabeta-methylene-adenosine 5'-tetraphosphate, betagamma-methylene adenosine 5'-tetraphosphate, gammadelta-methylene 5'-tetraphosphate, alphabeta-gammadelta-bismethylene-adenosine 5'-tetraphosphate, alphabeta-betagamma-bismethylene-adenosine 5'-tetraphosphate, and betagamma-gammadelta-bis(dichloro)methylene-adenosine 5'-tetraphosphate
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.08
adenosine 5'-tetraphosphate
-
pH 4.75, 50 mM sodium acetate, 5 mM CoCl2
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
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). Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
enzyme is stable at the extremes of pH for at least 30 min
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Guranowski, A.; Starzynska, E.; Barnes, L.D.; Robinson, A.K.; Liu, S.
Adenosine 5'-tetraphosphate phosphohydrolase activity is an inherent property of soluble exopolyphosphatase from yeast Saccharomyces cerevisiae
Biochim. Biophys. Acta
1380
232-238
1998
Saccharomyces cerevisiae
brenda
Small, G.D.; Cooper, C.
Purification and properties of nucleoside tetraphosphate hydrolase from rabbit muscle
Biochemistry
5
14-26
1966
Oryctolagus cuniculus
brenda
Guranowski, A.; Starzynska, E.; Brown, P.; Blackburn, G.M.
Adenosine 5'-tetraphosphate phosphohydrolase from yellow lupin seeds: purification to homogeneity and some properties
Biochem. J.
328
257-262
1997
Lupinus luteus
brenda
Guranowski, A.; Starzynska, E.; Pietrowska-Borek, M.; Jemielity, J.; Kowalska, J.; Darzynkiewicz, E.; Thompson, M.J.; Blackburn, G.M.
Methylene analogues of adenosine 5-tetraphosphate. Their chemical synthesis and recognition by human and plant mononucleoside tetraphosphatases and dinucleoside tetraphosphatases
FEBS J.
273
829-838
2006
Homo sapiens, Lupinus luteus
brenda
Amici, A.; Grolla, A.A.; Del Grosso, E.; Bellini, R.; Bianchi, M.; Travelli, C.; Garavaglia, S.; Sorci, L.; Raffaelli, N.; Ruggieri, S.; Genazzani, A.A.; Orsomando, G.
Synthesis and degradation of adenosine 5-tetraphosphate by nicotinamide and nicotinate phosphoribosyltransferases
Cell Chem. Biol.
24
553-564
2017
Homo sapiens
brenda
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