Information on EC 3.6.1.B13 - P1,P6-bis(5'-adenosyl)hexaphosphate (adenosine tetraphosphate-forming)

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.6.1.B13
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
P1,P6-bis(5'-adenosyl)hexaphosphate (adenosine tetraphosphate-forming)
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
P1,P5-bis(5'-adenosyl)pentaphosphate + H2O = adenosine 5'-tetraphosphate + AMP
show the reaction diagram
P1,P6-bis(5'-adenosyl)hexaphosphate + H2O = adenosine 5'-tetraphosphate + ADP
show the reaction diagram
SYSTEMATIC NAME
IUBMB Comments
P1,P6-bis(5'-adenosyl)hexaphosphate nucleotidohydrolase (adenosine tetraphosphate-forming)
-
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,P5-bis(5'-adenosyl)pentaphosphate + H2O
adenosine 5'-tetraphosphate + AMP
show the reaction diagram
P1,P6-bis(5'-adenosyl)hexaphosphate + H2O
adenosine 5'-tetraphosphate + ADP
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,P5-bis(5'-adenosyl)pentaphosphate + H2O
adenosine 5'-tetraphosphate + AMP
show the reaction diagram
Q99321
the function of the enzyme may be to eliminate potentially toxic dinucleoside polyphosphates during sporulation
-
-
?
P1,P6-bis(5'-adenosyl)hexaphosphate + H2O
adenosine 5'-tetraphosphate + ADP
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mn2+
optimal activity with 4-10 mM Mg2+ or 0.2 mM Mn2+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
F-
noncompetitive inhibitor
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
dithiothreitol
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.61
P1,P6-bis(5'-adenosyl)hexaphosphate
pH 7.6, 37°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
9.8
P1,P6-bis(5'-adenosyl)hexaphosphate
Arabidopsis thaliana
Q52K88
pH 7.6, 37°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
16
P1,P6-bis(5'-adenosyl)hexaphosphate
Arabidopsis thaliana
Q52K88
pH 7.6, 37°C
2615
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.08
F-
pH 6.9, 37°C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3.3
Ca2+
Saccharomyces cerevisiae
Q99321
pH 6.9, 37°C
0.07
fluoride
Arabidopsis thaliana
Q52K88
pH 7.6, 37°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
21443
x * 21443, calculation from sequence
26000
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 21443, calculation from sequence
monomer
1 * 26000, SDS-PAGE
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli and Saccharomyces cerevisiae
overexpressed in Escherichia coli
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expressed in log phase yeast cells