Information on EC 3.6.1.61 - diadenosine hexaphosphate hydrolase (ATP-forming)

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.6.1.61
-
RECOMMENDED NAME
GeneOntology No.
diadenosine hexaphosphate hydrolase (ATP-forming)
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
P1,P4-bis(5'-adenosyl)tetraphosphate + H2O = ATP + AMP
show the reaction diagram
P1,P5-bis(5'-adenosyl)pentaphosphate + H2O = ATP + ADP
show the reaction diagram
P1,P6-bis(5'-adenosyl)hexaphosphate + H2O = 2 ATP
show the reaction diagram
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Purine metabolism
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SYSTEMATIC NAME
IUBMB Comments
P1,P6-bis(5'-adenosyl)hexaphosphate nucleotidohydrolase (ATP-forming)
The enzyme requires the presence of the divalent cations (Mn2+, Mg2+, Zn2+, and Co2+). It hydrolyses P1,P4-bis(5-guanosyl) tetraphosphate very slowly [cf. EC 3.6.1.17, bis(5-nucleosyl)-tetraphosphatase (asymmetrical)].
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
P1,P4-bis(5'-adenosyl)tetraphosphate + H2O
ATP + AMP
show the reaction diagram
P1,P5-bis(5'-adenosyl)pentaphosphate + H2O
ATP + ADP
show the reaction diagram
P1,P6-bis(5'-adenosyl)hexaphosphate + H2O
2 ATP
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
P1,P6-bis(5'-adenosyl)hexaphosphate + H2O
2 ATP
show the reaction diagram
Q75UV1
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
Ndx1 activity requires the presence of the divalent cations Mn2+, Mg2+, Zn2+, and Co2+
additional information
Ca2+, Ni2+, and Cu2+ are not able to activate Ndx1
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
fluoride
non-competitive inhibition
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.07
P1,P4-bis(5'-adenosyl)tetraphosphate
pH 9.0, 37°C
0.36
P1,P5-bis(5'-adenosyl)pentaphosphate
pH 9.0, 37°C
0.0014
P1,P6-bis(5'-adenosyl)hexaphosphate
pH 7.0, 25°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.1
P1,P4-bis(5'-adenosyl)tetraphosphate
pH 9.0, 37°C
1
P1,P5-bis(5'-adenosyl)pentaphosphate
pH 9.0, 37°C
4.1
P1,P6-bis(5'-adenosyl)hexaphosphate
pH 7.0, 25°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.43
P1,P4-bis(5'-adenosyl)tetraphosphate
pH 9.0, 37°C
2.78
P1,P5-bis(5'-adenosyl)pentaphosphate
pH 9.0, 37°C
2929
P1,P6-bis(5'-adenosyl)hexaphosphate
pH 7.0, 25°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.013
ATP
pH 7.0, 25°C
0.041
dATP
pH 7.0, 25°C
0.424
fluoride
pH 7.0, 25°C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.08
fluoride
Thermus thermophilus
Q75UV1
pH 7.0, 25°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8
hydrolysis of P1,P6-bis(5'-adenosyl)hexaphosphate
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
70
hydrolysis of P1,P6-bis(5'-adenosyl)hexaphosphate
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.8
calculated from sequence
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
14170
1 * 14170, calculated from sequence
20000
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
1 * 14170, calculated from sequence
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2 - 12
25°C, stable
715466
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
95
pH 7.5, stable up to
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
overexpressed in Escherichia coli
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E46Q
2200fold reduction in kcat
E49Q
mutation has very little effect on activity
E50Q
130000fold reduction in kcat
W26S
no decrease in fluorescence intensity upon the addition of ATP
Show AA Sequence (155 entries)
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