Information on EC 3.6.1.B11 - multiple site diadenosine 5',5'''-P1,P6-hexaphosphate hydrolase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
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: Schizosaccharomyces pombe

EC NUMBER
COMMENTARY hide
3.6.1.B11
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
multiple site diadenosine 5',5'''-P1,P6-hexaphosphate hydrolase
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
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 (ADP-forming)
-
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,P5-bis(5'-adenosyl)pentaphosphate + H2O
ATP + ADP
show the reaction diagram
P1,P6-bis(5'-adenosyl)hexaphosphate + H2O
adenosine 5'-tetraphosphate + ADP
show the reaction diagram
additional information
?
-
the enzyme has limited activity on P1,P4-bis(5'-adenosyl)tetraphosphate and negligible activity on P1,P3-bis(5'-adenosyl)triphosphate, ADP-ribose, and NADH. Aps1 catalyzes the hydrolysis of mononucleotides with decreasing activity in order from p5A to AMP
-
-
-
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
ATP + ADP
show the reaction diagram
Q09790
-
-
-
?
P1,P6-bis(5'-adenosyl)hexaphosphate + H2O
adenosine 5'-tetraphosphate + ADP
show the reaction diagram
Q09790
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
1 mM CaCl2, 45% of the activity with 0.1-1 mM MnCl2
Co2+
1 mM CoCl2, 45% of the activity with 0.1-1 mM MnCl2
Mg2+
1 mM MgCl2, 45% of the activity with 0.1-1 mM MnCl2
Mn2+
optimal hydrolysis of P1,P6-bis(5'-adenosyl)hexaphosphate in the presence of 0.1-1 mM MnCl2. Gradual decrease to about 1/3 maximum activity at 5 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.022
P1,P5-bis(5'-adenosyl)pentaphosphate
pH 7.6, 37C
0.00219 - 0.019
P1,P6-bis(5'-adenosyl)hexaphosphate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.7
P1,P5-bis(5'-adenosyl)pentaphosphate
Schizosaccharomyces pombe
Q09790
pH 7.6, 37C
0.46 - 2
P1,P6-bis(5'-adenosyl)hexaphosphate
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
77
P1,P5-bis(5'-adenosyl)pentaphosphate
Schizosaccharomyces pombe
Q09790
pH 7.6, 37C
3954
2.23 - 105
P1,P6-bis(5'-adenosyl)hexaphosphate
2615
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.6
hydrolysis of P1,P6-bis(5'-adenosyl)hexaphosphate
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.1 - 8.1
pH 6.1: about 60% of maximal activity, pH 8.1: about 35% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
9.49
calculated from sequence
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
23724
1 * 23724, calculated from sequence
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
1 * 23724, calculated from sequence
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
wild-type Aps1, His10-tagged Aps1, and truncated forms of Aps1
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cloning of His10-tagged aps1, aps1DELTA2-19, and aps1DELTA2-31, expression in Escherichia coli
-
expression in Escherichia coli
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E93Qaps1DELTA2-19
-
mutant has 0.0003 times the hydrolase activity toward P1,P6-bis(5'-adenosyl)hexaphosphate as compared to wild-type enzyme