Information on EC 3.6.1.14 - adenosine-tetraphosphatase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Mark a special word or phrase in this record:
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


The expected taxonomic range for this enzyme is: Eukaryota

EC NUMBER
COMMENTARY
3.6.1.14
-
RECOMMENDED NAME
GeneOntology No.
adenosine-tetraphosphatase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
adenosine 5'-tetraphosphate + H2O = ATP + phosphate
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
phosphorous acid anhydride hydrolysis
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Purine metabolism
-
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.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
adenosinetetraphosphatase
-
-
-
-
nucleoside tetraphosphatase
-
-
p4A phosphohydrolase
-
-
-
-
phosphatase, adenosine tetra-
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
37289-26-2
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
yellow lupin
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
adenosine 5'-pentaphosphate + H2O
?
show the reaction diagram
-
-
-
-
?
adenosine 5'-pentaphosphate + H2O
?
show the reaction diagram
-
hydrolyzed 18fold more slowly than adenosine 5'-tetraphosphate, hydrolyzed at 1/200 the rate of adenosine 5'-tetraphosphate
-
-
?
adenosine 5'-tetraphosphate + H2O
ATP + phosphate
show the reaction diagram
-
-
-
?
adenosine 5'-tetraphosphate + H2O
ATP + phosphate
show the reaction diagram
-
-
-
?
adenosine 5'-tetraphosphate + H2O
ATP + phosphate
show the reaction diagram
-
-
-
?
alpha-beta-methylene-adenosine 5'-tetraphosphate + H2O
alpha-beta-methylene-adenosine 5'-triphosphate + phosphate
show the reaction diagram
-
-
-
-
?
guanosine tetraphosphate + H2O
GTP + phosphate
show the reaction diagram
-
-
-
?
guanosine tetraphosphate + H2O
GTP + phosphate
show the reaction diagram
-
-
-
?
inosine tetraphosphate + H2O
ITP + phosphate
show the reaction diagram
-
-
-
?
inosine tetraphosphate + H2O
ITP + phosphate
show the reaction diagram
-
-
-
?
tripolyphosphate + H2O
diphosphate + phosphate
show the reaction diagram
-
-
-
?
tripolyphosphate + H2O
diphosphate + phosphate
show the reaction diagram
-
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Co2+
-
divalent cations activate hydrolysis of adenosine 5'-tetraphosphate in the order of decreasing effectiveness: Co2+, Mn2+, Mg2+, 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 metal ion, Mg2+, Co2+, Ni2+ or Mn2+, required
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+
-
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 metal ion, Mg2+, Co2+, Ni2+ or Mn2+ required
Mn2+
-
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 metal ion, Mg2+, Co2+, Ni2+ or Mn2+ required
Ni2+
-
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 metal ion, Mg2+, Co2+, Ni2+ or Mn2+ required
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
Ammonium molybdate
-
-
N-ethylmaleimide
-
-
p-hydroxymercuribenzoate
-
-
sodium o-vanadate
-
-
tripolyphosphate
-
competitive inhibitor of adenosine 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
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0027
-
adenosine 5'-tetraphosphate
-
-
0.003
-
adenosine 5'-tetraphosphate
-
-
0.08
-
adenosine 5'-tetraphosphate
-
pH 4.75, 50 mM sodium acetate, 5 mM CoCl2
0.0034
-
inosine tetraphosphate
-
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
723
-
adenosine 5'-tetraphosphate
-
-
40
-
adenosine-5'-pentaphosphate
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
20.83
-
-
-
additional information
-
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
3.8
7.2
-
50% of maximal activity at pH 3.8 and 7.2
7.6
9.4
-
50% of maximal activity at pH 7.6 and 9.4
PDB
SCOP
CATH
ORGANISM
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25000
-
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 45000, SDS-PAGE
monomer
-
1 * 25000, SDS-PAGE
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
-
enzyme is stable at the extremes of pH for at least 30 min
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20°C, 6 months, no loss of activity
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE