Information on EC 3.6.1.60 - diadenosine hexaphosphate hydrolase (AMP-forming)

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The expected taxonomic range for this enzyme is: Homo sapiens

EC NUMBER
COMMENTARY hide
3.6.1.60
-
RECOMMENDED NAME
GeneOntology No.
diadenosine hexaphosphate hydrolase (AMP-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'-pentaphosphate + AMP
show the reaction diagram
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.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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
weak activity
-
-
?
P1,P5-bis(5'-adenosyl)pentaphosphate + H2O
adenosine 5'-tetraphosphate + AMP
show the reaction diagram
P1,P6-bis(5'-adenosyl)hexaphosphate + H2O
adenosine 5'-pentaphosphate + AMP
show the reaction diagram
additional information
?
-
the enzyme also catalyses the hydrolysis of diphosphoinositol pentakisphosphate
-
-
-
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
Q8NFP7, Q96G61
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
show the reaction diagram
Q8NFP7, Q96G61
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 hide
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; 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; 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; 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; 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
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
fluoride
non-competitive inhibition; non-competitive inhibition
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0077 - 0.05
P1,P5-bis(5'-adenosyl)pentaphosphate
0.0059 - 0.019
P1,P6-bis(5'-adenosyl)hexaphosphate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.4 - 0.8
P1,P5-bis(5'-adenosyl)pentaphosphate
0.16 - 0.5
P1,P6-bis(5'-adenosyl)hexaphosphate
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
8 - 55
P1,P5-bis(5'-adenosyl)pentaphosphate
3954
10.5 - 84.7
P1,P6-bis(5'-adenosyl)hexaphosphate
2615
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.013
fluoride
pH 7.6, 37°C; pH 7.6, 37°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.6
assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5 - 9
pH 7.5: about 55% of maximal activity, pH 8.5-9: maximal activity; pH 7.5: about 60% of maximal activity, pH 9: about 90% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
; high activity
Manually annotated by BRENDA team
; low activity
Manually annotated by BRENDA team
; low activity
Manually annotated by BRENDA team
; low activity
Manually annotated by BRENDA team
; high activity
Manually annotated by BRENDA team
; low activity
Manually annotated by BRENDA team
; high activity
Manually annotated by BRENDA team
low activity
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
18500
x * 18500, calculation from sequence
18559
x * 18559, calculation from sequence
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 18500, calculation from sequence; x * 18559, calculation from sequence
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
S39N
a polymorphism of hAps1 leads to the point mutation S39N
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
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