Information on EC 3.6.1.17 - bis(5'-nucleosyl)-tetraphosphatase (asymmetrical)

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
3.6.1.17
-
RECOMMENDED NAME
GeneOntology No.
bis(5'-nucleosyl)-tetraphosphatase (asymmetrical)
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
P1,P4-bis(5'-guanosyl) tetraphosphate + H2O = GTP + GMP
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphorous acid anhydride hydrolysis
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Purine metabolism
-
-
Pyrimidine metabolism
-
-
SYSTEMATIC NAME
IUBMB Comments
P1,P4-bis(5'-nucleosyl)-tetraphosphate nucleotidohydrolase
Also acts on bis(5'-xanthosyl)-tetraphosphate and, more slowly, on bis(5'-adenosyl)-tetraphosphate and bis(5'-uridyl)-tetraphosphate [cf. EC 3.6.1.41 bis(5'-nucleosyl)-tetraphosphatase (symmetrical)]
CAS REGISTRY NUMBER
COMMENTARY hide
37289-29-5
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
brine shrimp
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
serovar 434/Bu
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
marrow
-
-
Manually annotated by BRENDA team
sunflower
-
-
Manually annotated by BRENDA team
Lupinus sp.
-
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
firefly
-
-
Manually annotated by BRENDA team
Scenedesmus sp.
-
-
-
Manually annotated by BRENDA team
tomato
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(2'-pdA)AppppA + H2O
?
show the reaction diagram
-
cleavage to produce ATP and 2'-deoxyadenylated AMP rather than 2'-deoxyadenylated ATP + AMP occurs with a ratio of 60:40 with the wild-type enzyme and the mutant enzymes R54Q, E58D and E125Q. With the mutants R54Q, E58D and E125Q, releasing ATP is increased to 70% of total hydrolysis. Activity of mutants E55Q, E59D and E59Q is to low to be detected
-
-
?
2'-deoxyadenosine adenosine tetraphosphate + H2O
ATP + 2'-dAMP + 2'-dATP + AMP
show the reaction diagram
-
-
80% dAMP, 20% AMP
?
2-oxo-dATP + H2O
?
show the reaction diagram
5',5''-diadenosine pentaphosphate + H2O
ATP + ADP
show the reaction diagram
-
42% of the activity with 5',5''-diadenosine tetraphosphate
-
?
5',5''-diadenosine tetraphosphate + H2O
ATP + AMP
show the reaction diagram
-
-
-
?
5',5'-diadenosine hexaphosphate + H2O
2 ATP
show the reaction diagram
diadenosine hexaphosphate is efficiently hydrolysed to ATP only at pH 7.5 with 20 mM Mg2+
-
-
?
5',5'-diadenosine pentaphosphate + H2O
ATP + ADP
show the reaction diagram
-
-
-
?
5',5'-diadenosine tetraphosphate + H2O
ATP + AMP
show the reaction diagram
8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
show the reaction diagram
A-5'-p-alpha,beta,alpha',beta'-bis(oxymethylene)p-5'-A + H2O
2 alpha,beta-oxymethylene-ADP
show the reaction diagram
adenosine-5'-pentaphospho-5'-guanosine + H2O
?
show the reaction diagram
-
-
-
?
adenosine-5'-tetraphospho-5'-guanosine + H2O
?
show the reaction diagram
-
-
-
?
Ap6A + H2O
Ap5 + AMP
show the reaction diagram
-
-
-
-
?
Ap6A + H2O
ATP + ATP
show the reaction diagram
-
7% of the activity with Ap4A
-
-
?
betabeta'-methyleneoxy-Ap4A + H2O
AMP + beta,gamma-methyleneoxy-ATP
show the reaction diagram
dATP + H2O
?
show the reaction diagram
dGTP + H2O
?
show the reaction diagram
di-2,6-diaminopurine beta-D-ribofuranoside tetraphosphate + H2O
?
show the reaction diagram
-
-
-
-
?
diadenosine 5',5''''-P1,P4-tetraphosphate + H2O
AMP + ATP
show the reaction diagram
diadenosine 5',5''-P1,P4-tetraphosphate + H2O
ATP + AMP
show the reaction diagram
diadenosine 5',5''-P1,P5-pentaphosphate + H2O
adenosine 5'-tetraphosphate + AMP
show the reaction diagram
-
-
-
-
?
diadenosine 5',5''-P1,P5-pentaphosphate + H2O
ATP + ADP
show the reaction diagram
-
19% of the activity with Ap4A
-
-
?
diadenosine 5',5'-P1,P4-tetraphosphate + H2O
ATP + AMP
show the reaction diagram
diadenosine 5',5'-P1,P4-tetraphosphate + H2O
ATP + AMP + ?
show the reaction diagram
key enzyme controlling the in vivo concentration of diadenosine 5',5'-P1,P4 tetraphosphate (Ap4A) - an important signaling molecule involved in regulation of DNA replication and repair, signaling in stress response and apoptosis
-
-
?
diadenosine 5',5'-P1,P5-pentaphosphate + H2O
ATP + ADP
show the reaction diagram
-
-
-
?
diguanosine 5',5'-P1,P4-tetraphosphate + H2O
GTP + GMP
show the reaction diagram
-
-
-
?
DNA + H2O
?
show the reaction diagram
-
poor substrate
-
-
?
P1,P3-bis(5'-adenosyl)triphosphate + H2O
AMP + ADP
show the reaction diagram
-
-
-
?
P1,P3-bis(5'-guanosyl) triphosphate + H2O
?
show the reaction diagram
-
poor substrate
-
-
?
P1,P4-bis(5'-(2'-deoxy)adenosyl) tetraphosphate + H2O
?
show the reaction diagram
-
-
-
-
?
P1,P4-bis(5'-adenosyl) tetraphosphate + H2O
ATP + AMP
show the reaction diagram
P1,P4-bis(5'-adenosyl)tetraphosphate + H2O
AMP + ATP
show the reaction diagram
P1,P4-bis(5'-guanosyl)tetraphosphate + H2O
GTP + GMP
show the reaction diagram
P1,P4-bis(5'-uridyl) tetraphosphate + H2O
UTP + UMP
show the reaction diagram
P1,P4-bis(5'-xanthosyl) tetraphosphate + H2O
XTP + XMP
show the reaction diagram
P1,P5-bis(5'-adenosyl) pentaphosphate + H2O
ADP + ATP
show the reaction diagram
P1,P5-bis(5'-adenosyl) pentaphosphate + H2O
ATP + ADP
show the reaction diagram
P1,P5-bis(5'-adenosyl)pentaphosphate + H2O
AMP + adenosine 5'-tetraphosphate
show the reaction diagram
P1,P6-bis(5'-adenosyl) hexaphosphate + H2O
2 ATP
show the reaction diagram
P1,P6-bis(5'-adenosyl) hexaphosphate + H2O
ATP
show the reaction diagram
p4A + H2O
ATP + phosphate
show the reaction diagram
-
14% of the activity with Ap4A
-
-
?
p5A + H2O
ATP + diphosphate
show the reaction diagram
-
29% of the activity with Ap4A
-
-
?
RNA + H2O
?
show the reaction diagram
-
poor substrate
-
-
?
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
5',5'-diadenosine tetraphosphate + H2O
ATP + AMP
show the reaction diagram
Q4V6M1
-
-
-
?
diadenosine 5',5'-P1,P4-tetraphosphate + H2O
ATP + AMP
show the reaction diagram
diadenosine 5',5'-P1,P4-tetraphosphate + H2O
ATP + AMP + ?
show the reaction diagram
Q9C6Z2
key enzyme controlling the in vivo concentration of diadenosine 5',5'-P1,P4 tetraphosphate (Ap4A) - an important signaling molecule involved in regulation of DNA replication and repair, signaling in stress response and apoptosis
-
-
?
diadenosine 5',5'-P1,P5-pentaphosphate + H2O
ATP + ADP
show the reaction diagram
Q9C6Z2
-
-
-
?
diguanosine 5',5'-P1,P4-tetraphosphate + H2O
GTP + GMP
show the reaction diagram
Q9C6Z2
-
-
-
?
P1,P4-bis(5'-adenosyl) tetraphosphate + H2O
ATP + AMP
show the reaction diagram
P1,P4-bis(5'-guanosyl)tetraphosphate + H2O
GTP + GMP
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Cd2+
no activity in the presence of 1.0 mM Cd2+, weak enzyme activation at 5 mM (4.% compared to 1.5 mM Mn2+)
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,2,3,4-tetra(adenosine-5'-O-phospho)erythritol
-
-
1,2,3,4-tetra(adenosine-5'-O-phosphorothio)erythritol
1,2,3-tri(adenosine-5'-O-phosphorothio)glycerol
1,3-di(adenosine-5'-O-phospho)-2-phospho-glycerol
-
-
1,3-di(adenosine-5'-O-phospho)-2-phosphorothio-glycerol
1,3-di(adenosine-5'-O-phospho)glycerol
-
-
1,4-di(adenosine-5'-O-phospho)erythritol
1,4-di(adenosine-5'-O-phosphorothio)erythritol
1,4-dihydroxy-5,8-bis[(4-methylphenyl)amino]anthracene-9,10-dione
NSC86169
2-((8-hydroxy-4-(4-methyl-2-sulfoanilino)-9,10-dioxo-9,10-dihydro-1-anthracenyl)amino)-5-methylbenzenesulfonic acid
NSC51531, competitive inhibitor
2-[2-[(4-aminophenyl)amino]-6-phenylpyrimidin-4-yl]phenol
NSC232476
5-hydroxy-1,4-bis[(4-methylphenyl)amino]anthracene-9,10-dione
NSC300513
5-methyl-2-[[4-(methylamino)-9,10-dioxo-9,10-dihydroanthracen-1-yl]amino]benzenesulfonate
NSC401611
A-5'-p-alpha,beta,alpha',beta'-bis(oxymethylene)p-5'-A
A-5'-p-beta,beta'-methyleneoxy-p-5'-A
adenosine 5'-tetraphosphate
di(adenosine-5'-O-phosphorothio)-di(adenosine-5'-phospho)pentaerythritol
-
-
diadenosine 5',5'''-P1,P4-tetraphosphate
-
-
diadenosine triphosphate
-
competitive, also phosphonate analogues of the substance
fluoride
fructose-6-phosphate
-
slight inhibition
glycerol phosphate
20 mM, 46.1% residual activity
guanosine 5'-tetraphosphate
inositol 1-[(phosphorylmethyl)phosphonic acid]-2,3,4,5,6-pentaphosphate
competitive
inositol 1-[(phosphorylmethyl)phosphonic acid]-2,3,5,6-tetraphosphate
competitive
inositol 4-butyl-1-[(phosphorylmethyl)phosphonic acid]-2,3,5,6-tetraphosphate
competitive
iodoacetic acid
10 mM, 58.8% residual activity
Ionic strength
-
significant inhibition at high ionic strength
-
N-ethylmaleimide
1 mM, 73.8% residual activity
p-mercuribenzoate
-
-
perylene-3,4,9,10-tetracarboxylic acid
NSC89768
phosphate
-
inhibitory above 30 mM
trisodium phosphate
20 mM, 24.8% residual activity
-
uridine 5'-tetraphosphate
-
Ki in nanomolar range
additional information
NSC113427, NSC133815, and NSC305522, do not exhibit any enzyme inhibition at concentrations in excess of 0.1 mM
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
beta-mercaptoethanol
-
slight activation
dithiothreitol
-
slight activation
EDTA
-
able to reverse Zn2+ inhibition
fructose 2,6-diphosphate
-
able to reverse Zn2+ inhibition, ineffective on the enzyme without Zn2+
phosphate
-
activating below 30 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.3846
2-oxo-dATP
in 50 mM Tris-HCl (pH 8.0), 5 mM MgCl2, 20 mM NaCl, 1 mM dithiothreitol, 0.2 mg/ml bovine serum albumin, at 37C
0.0006 - 0.003
5',5''-diadenosine tetraphosphate
-
0.015
5',5'-diadenosine hexaphosphate
pH 7.5, 20 mM Mg2+
0.009 - 0.012
5',5'-diadenosine tetraphosphate
0.0986
8-oxo-dGTP
in 50 mM Tris-HCl (pH 8.0), 5 mM MgCl2, 20 mM NaCl, 1 mM dithiothreitol, 0.2 mg/ml bovine serum albumin, at 37C
0.0041 - 10
Ap4A
0.098
Ap5A
-
pH 7.4, 37C
0.04
Ap6A
-
pH 7.4, 37C
0.1143
dATP
in 50 mM Tris-HCl (pH 8.0), 5 mM MgCl2, 20 mM NaCl, 1 mM dithiothreitol, 0.2 mg/ml bovine serum albumin, at 37C
0.182
dGTP
in 50 mM Tris-HCl (pH 8.0), 5 mM MgCl2, 20 mM NaCl, 1 mM dithiothreitol, 0.2 mg/ml bovine serum albumin, at 37C
0.007
diadenosine 5',5''''-P1,P4-tetraphosphate
in 50 mM Tris-HCl (pH 8.0), 5 mM MgCl2, 20 mM NaCl, 1 mM dithiothreitol, 0.2 mg/ml bovine serum albumin, at 37C
0.005 - 0.407
diadenosine 5',5''-P1,P4-tetraphosphate
0.002 - 0.0025
diadenosine 5',5'-P1,P4-tetraphosphate
0.0007 - 0.054
P1,P4-bis(5'-adenosyl) tetraphosphate
0.14
P1,P4-bis(5'-adenosyl)tetraphosphate
pH 8.0, 50C, presence of 1 mM Mn2+
0.001 - 1.03
P1,P4-bis(5'-guanosyl) tetraphosphate
0.01 - 0.011
P1,P4-bis(5'-uridyl) tetraphosphate
0.016 - 0.018
P1,P4-bis(5'-xanthosyl) tetraphosphate
0.183
P1,P5-bis(5'-adenosyl) pentaphosphate
in 50 mM Tris-HCl, 100 mM KCl, 5 mM MgCl2, pH 7.6, at 25C
0.19
P1,P5-bis(5'-adenosyl)pentaphosphate
pH 8.0, 50C, presence of 1 mM Mn2+
0.089
P1,P6-bis(5'-adenosyl) hexaphosphate
in 50 mM Tris-HCl, 100 mM KCl, 5 mM MgCl2, pH 7.6, at 25C
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.51
2-oxo-dATP
Caenorhabditis elegans
Q9U2M7
in 5 0mM Tris-HCl (pH 8.0), 5 mM MgCl2, 20 mM NaCl, 1 mM dithiothreitol, 0.2 mg/ml bovine serum albumin, at 37C
0.013 - 0.08
5',5''-diadenosine tetraphosphate
-
4
5',5'-diadenosine hexaphosphate
Drosophila melanogaster
Q4V6M1
pH 7.5, 20 mM Mg2+
13 - 43
5',5'-diadenosine tetraphosphate
0.58
8-oxo-dGTP
Caenorhabditis elegans
Q9U2M7
in 50 mM Tris-HCl (pH 8.0), 5 mM MgCl2, 20 mM NaCl, 1 mM dithiothreitol, 0.2 mg/ml bovine serum albumin, at 37C
0.00024 - 40.8
Ap4A
0.37
dATP
Caenorhabditis elegans
Q9U2M7
in 50 mM Tris-HCl (pH 8.0), 5 mM MgCl2, 20 mM NaCl, 1 mM dithiothreitol, 0.2 mg/ml bovine serum albumin, at 37C
0.53
dGTP
Caenorhabditis elegans
Q9U2M7
in 50 mM Tris-HCl (pH 8.0), 5 mM MgCl2, 20 mM NaCl, 1 mM dithiothreitol, 0.2 mg/ml bovine serum albumin, at 37C
27
diadenosine 5',5''''-P1,P4-tetraphosphate
Caenorhabditis elegans
Q9U2M7
in 50 mM Tris-HCl (pH 8.0), 5 mM MgCl2, 20 mM NaCl, 1 mM dithiothreitol, 0.2 mg/ml bovine serum albumin, at 37C
0.68 - 3.25
diadenosine 5',5''-P1,P4-tetraphosphate
2.5 - 3.6
P1,P4-bis(5'-adenosyl) tetraphosphate
0.055
P1,P4-bis(5'-adenosyl)tetraphosphate
Myxococcus xanthus
Q1DC62
pH 8.0, 50C, presence of 1 mM Mn2+
1.4
P1,P5-bis(5'-adenosyl) pentaphosphate
Aquifex aeolicus
O66548
in 50 mM Tris-HCl, 100 mM KCl, 5 mM MgCl2, pH 7.6, at 25C
0.035
P1,P5-bis(5'-adenosyl)pentaphosphate
Myxococcus xanthus
Q1DC62
pH 8.0, 50C, presence of 1 mM Mn2+
0.2
P1,P6-bis(5'-adenosyl) hexaphosphate
Aquifex aeolicus
O66548
in 50 mM Tris-HCl, 100 mM KCl, 5 mM MgCl2, pH 7.6, at 25C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.3
2-oxo-dATP
Caenorhabditis elegans
Q9U2M7
in 50 mM Tris-HCl (pH 8.0), 5 mM MgCl2, 20 mM NaCl, 1 mM dithiothreitol, 0.2 mg/ml bovine serum albumin, at 37C
26813
5.9
8-oxo-dGTP
Caenorhabditis elegans
Q9U2M7
in 50 mM Tris-HCl (pH 8.0), 5 mM MgCl2, 20 mM NaCl, 1 mM dithiothreitol, 0.2 mg/ml bovine serum albumin, at 37C
2299
3.3
dATP
Caenorhabditis elegans
Q9U2M7
in 50 mM Tris-HCl (pH 8.0), 5 mM MgCl2, 20 mM NaCl, 1 mM dithiothreitol, 0.2 mg/ml bovine serum albumin, at 37C
140
2.9
dGTP
Caenorhabditis elegans
Q9U2M7
in 50 mM Tris-HCl (pH 8.0), 5 mM MgCl2, 20 mM NaCl, 1 mM dithiothreitol, 0.2 mg/ml bovine serum albumin, at 37C
219
3900
diadenosine 5',5''''-P1,P4-tetraphosphate
Caenorhabditis elegans
Q9U2M7
in 50 mM Tris-HCl (pH 8.0), 5 mM MgCl2, 20 mM NaCl, 1 mM dithiothreitol, 0.2 mg/ml bovine serum albumin, at 37C
25173
4.4 - 220
diadenosine 5',5''-P1,P4-tetraphosphate
14480
46
P1,P4-bis(5'-adenosyl) tetraphosphate
Aquifex aeolicus
O66548
in 50 mM Tris-HCl, 100 mM KCl, 5 mM MgCl2, pH 7.6, at 25C
1417
0.4
P1,P4-bis(5'-adenosyl)tetraphosphate
Myxococcus xanthus
Q1DC62
pH 8.0, 50C, presence of 1 mM Mn2+
8171
7.6
P1,P5-bis(5'-adenosyl) pentaphosphate
Aquifex aeolicus
O66548
in 50 mM Tris-HCl, 100 mM KCl, 5 mM MgCl2, pH 7.6, at 25C
13216
0.18
P1,P5-bis(5'-adenosyl)pentaphosphate
Myxococcus xanthus
Q1DC62
pH 8.0, 50C, presence of 1 mM Mn2+
3954
2.2
P1,P6-bis(5'-adenosyl) hexaphosphate
Aquifex aeolicus
O66548
in 50 mM Tris-HCl, 100 mM KCl, 5 mM MgCl2, pH 7.6, at 25C
13217
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.031
1,2,3,4-tetra(adenosine-5'-O-phospho)erythritol
-
pH 7.6, 30C
0.013 - 0.018
1,2,3,4-tetra(adenosine-5'-O-phosphorothio)erythritol
0.017 - 0.037
1,2,3-tri(adenosine-5'-O-phosphorothio)glycerol
0.066
1,3-di(adenosine-5'-O-phospho)-2-phospho-glycerol
-
pH 7.6, 30C
0.025 - 0.032
1,3-di(adenosine-5'-O-phospho)-2-phosphorothio-glycerol
0.109
1,3-di(adenosine-5'-O-phospho)glycerol
-
pH 7.6, 30C
0.0085 - 0.142
1,4-di(adenosine-5'-O-phospho)erythritol
0.00015 - 0.0015
1,4-di(adenosine-5'-O-phosphorothio)erythritol
0.00109
2-((8-hydroxy-4-(4-methyl-2-sulfoanilino)-9,10-dioxo-9,10-dihydro-1-anthracenyl)amino)-5-methylbenzenesulfonic acid
in 100 mM Tris-acetate, pH 7.7, 5 mM magnesium acetate, and 5% DMSO, at 25C
0.005
2-[2-[(4-aminophenyl)amino]-6-phenylpyrimidin-4-yl]phenol
Ki about 0.005 mM, in 100 mM Tris-acetate, pH 7.7, 5 mM magnesium acetate, and 5% (v/v) DMSO, at 25C
0.00289
5-methyl-2-[[4-(methylamino)-9,10-dioxo-9,10-dihydroanthracen-1-yl]amino]benzenesulfonate
in 100 mM Tris-acetate, pH 7.7, 5 mM magnesium acetate, and 5% (v/v) DMSO, at 25C
0.0015 - 0.0025
A-5'-p-alpha,beta,alpha',beta'-bis(oxymethylene)p-5'-A
0.0021 - 0.0022
A-5'-p-beta,beta'-methyleneoxy-p-5'-A
0.00001
adenosine 5'-tetraphosphate
-
pH 7.8, 25C
0.025 - 0.3
Ca2+
0.0037
di(adenosine-5'-O-phosphorothio)-di(adenosine-5'-phospho)pentaerythritol
-
pH 7.6, 30C
0.003 - 1
F-
0.02
fluoride
-
-
0.01
guanosine 5'-tetraphosphate
-
-
0.00011
inositol 1-[(phosphorylmethyl)phosphonic acid]-2,3,4,5,6-pentaphosphate
pH not specified in the publication, temperature not specified in the publication
0.00027
inositol 1-[(phosphorylmethyl)phosphonic acid]-2,3,5,6-tetraphosphate
pH not specified in the publication, temperature not specified in the publication
0.000023
inositol 4-butyl-1-[(phosphorylmethyl)phosphonic acid]-2,3,5,6-tetraphosphate
pH not specified in the publication, temperature not specified in the publication
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.02
fluoride
Drosophila melanogaster
Q4V6M1
in presence of Mg2+
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0001
-
crude extract
0.00022
-
crude extract
0.001
-
crude extract
0.0015
-
crude extract
0.002
-
crude extract
0.0074
-
crude exctract
0.02
-
crude extract
0.023
-
partially purified enzyme
0.2
-
purified enzyme
0.276
-
partially purified enzyme
0.436
-
partially purified enzyme
5.9
Mn2+ concentration 0.15 mM
13.5
-
purified enzyme
18.5
-
purified enzyme
19.2
Mn2+ concentration 0.75 mM
27
maximal activity of the enzyme coincides with total Mn2+ and Ap4A concentrations of 1 mM, at such concentrations the Mn(Ap4A) complex dominates and the concentration of its components Mn2+ = Ap4A are 0.083 mM, an excess of either Mn2+ or Ap4A over Mn(Ap4A) results in a decrease of the reaction rate
31.1
Mn2+ concentration 1.5 mM
52
-
purified enzyme
55.2
Mn2+ concentration 3.5 mM
70.5
Mn2+ concentration 6.5 mM
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 7.5
activity depends on the substrate and the divalent cation
6.5 - 9
-
very broad optimum range
7 - 8
-
degradation of Ap4A
7 - 8.5
-
depending on tissue
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.1 - 8.6
-
pH 6.1: about 75% of maximal activity, pH 8.6: about 10% of maximal activity, degradation of Ap4A
6.5 - 8
-
50% of maximal activity at pH 6.5 and at pH 8.0, hydrolysis of Ap4A
6.5 - 9.8
-
35% activity at pH 6.5 and 80% activity at pH 9.8
6.5 - 8.5
-
half maximum activity
6.5 - 9.8
Scenedesmus sp.
-
35% activity at pH 6.5 and 80% activity at pH 9.8
6.8 - 9.5
in the presence of 3.5 mM Mn2+, the enzyme is active over a wide pH range
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25 - 40
broad optimum
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 60
65% of maximal activity at 52C
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.1
deduced pI from amino acid sequence
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
undeveloped
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
bound to prostasome-membranes through a GPI-anchor
Manually annotated by BRENDA team
present on surface of vascular endothelium
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
isolated mitochondria used
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
14500
-
gel filtration
16000
-
SDS-PAGE
17000
x * 17000, SDS-PAGE
17500
-
gel filtration
18000 - 19000
Lupinus sp.
-
SDS-PAGE, MW depends on subspecies
18000
-
SDS-PAGE, immunoblot
19000
-
gel filtration
19120
-
wild-type enzyme, MALDI-MS
19200
-
SDS-PAGE, gel filtration
19800
-
gel filtration
19900 - 22000
-
gel filtration, exact MW depending on tissue
20000 - 26000
Scenedesmus sp.
-
gel filtration, MW depends on subspecies
21000
-
gel filtration
21670
by electrospray ionization quadrupole time-of-flight mass spectrometry
22980
Lupinus sp.
-
calculated from DNA sequence
49000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 17000, SDS-PAGE
monomer
-
1 * 16000, SDS-PAGE, gel filtration
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
free and ATP-bound enzyme, hanging drop vapor diffusion method, using 0.1 M Tris-HCl pH 7.6, 29% (w/v) PEG 3350, and 0.75 M NaCl (free enzyme) or 1 ml 0.1 M Tris-HCl pH 8.8, 25% (w/v) PEG 3350, and 0.2 M NaCl (ATP-bound enzyme)
sitting-drop vapour diffusion, crystals diffract to a minimum d-spacing of 2 A and belong to either space group C222 or C222(1)
-
structures of both apo- and ligand-bound CT771, to 2.6 A and 1.9 A resolution, respectively. The structure shows a alphabetaalpha-sandwich motif with many conserved elements lining the putative Nudix active site
-
structure determined by NMR spectroscopy
-
structure of wild-type and E58A mutant human Ap4A hydrolase, to 2.7 and 2.1 A resolution, respectively. Similar to the canonical Nudix fold, human Ap4A hydrolase shows the common alphabetaalpha-sandwich architecture. Two sulfate ions and one diphosphate coordinated with some conserved residues are observed in the active cleft
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 10
-
stable
209893
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
5 min, 18% inactivation; 5 min, complete inactivation
45
-
5 min, 69% inactivation
60
20 min, 55% remaining activity
70
10 min, 39% of initial activity
95
20 min, 1 mM Mn2+, a little amount of activity is remaining
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C crude salt fraction, 2-3 days
-
-20C, low ionic strength solution, several months, no loss of activity
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
by affinity chromatography by means of nickel-nitrilotriacetic acid agarose
HisTrap FF column chromatography and Superdex 75 gel filtration
partial
recombinant His-tagged Apf from Spodoptera frugiperda Sf21 cells by nickel affinity chromatography with removal of the His-tag
symmetrical Ap4A hydrolase is partially purified from Escherichia coli
-
Toyopearl SuperQ-650M column chromatography, Resource Q column chromatography, Bio-Scale CHT2-I column chromatography, and Superdex 75 gel filtration
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, sequence comparison, expression of His-tagged Apf in Spodoptera frugiperda Sf21 cells, expression of EGFP-tagged enzyme in Drosophila melanbogaster Mel-2 cells
expressed in Escherichia coli
Lupinus sp.
-
expressed in Escherichia coli BL21(DE3)T cells
expressed in Escherichia coli BL21-CodonPlus (DE3)-RIL cells
expression in Escherichia coli
expression in Escherichia coli, mutant enzymes Y27A, Y27D, H31A, H31V, W32G, K36M, H38G, H38K, E52Q, E56Q, Y76A, Y76/Y121A, K79M, K81M, K83M, E103Q, Y121A
-
expression in insect cells
fused to glutathione S-transferase and expressed in E. coli
-
overexpression in Escherichia coli
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E103Q
-
turnover-number for hydrolysis of Ap4A is 3.2% of that of the wild-type enzyme, KM-value is 66% of the wild-type value
E52Q
-
turnover-number for hydrolysis of Ap4A is 0.02% of that of the wild-type enzyme, KM-value is 60% of the wild-type value
E56Q
-
turnover-number for hydrolysis of Ap4A is 0.001% of that of the wild-type enzyme, KM-value is 90% of the wild-type value
H31A
-
turnover-number for hydrolysis of Ap4A is 52% of that of the wild-type enzyme, KM-value is 8.3fold higher than the KM-value of the wild-type enzyme
H31V
-
turnover-number for hydrolysis of Ap4A is 61% of that of the wild-type enzyme, KM-value is 12.5fold higher than the KM-value of the wild-type enzyme
H38G
-
turnover-number for hydrolysis of Ap4A is 135% of that of the wild-type enzyme, KM-value is 66% of the wild-type value
H38K
-
turnover-number for hydrolysis of Ap4A is 135% of that of the wild-type enzyme, KM-value is 47% of the wild-type value
K36M
-
turnover-number for hydrolysis of Ap4A is 9% of that of the wild-type enzyme, KM-value is 1.5fold higher than the KM-value of the wild-type enzyme
K79M
-
turnover-number for hydrolysis of Ap4A is 0.7% of that of the wild-type enzyme, KM-value is 1.7fold higher than the KM-value of the wild-type enzyme
K81M
-
turnover-number for hydrolysis of Ap4A is 130% of that of the wild-type enzyme, KM-value is 2.3fold higher than the KM-value of the wild-type enzyme
K83M
-
turnover-number for hydrolysis of Ap4A is 2.6% of that of the wild-type enzyme, KM-value is 15.9fold higher than the KM-value of the wild-type enzyme
Y121A
-
turnover-number for hydrolysis of Ap4A is 61% of that of the wild-type enzyme, KM-value is 8.5fold higher than the KM-value of the wild-type enzyme
Y27A
-
turnover-number for hydrolysis of Ap4A is 113% of that of the wild-type enzyme, KM-value is 1.25fold higher than the KM-value of the wild-type enzyme
Y27D
-
turnover-number for hydrolysis of Ap4A is 126% of that of the wild-type enzyme, KM-value is 1.8fold higher than the KM-value of the wild-type enzyme
Y76A
-
turnover-number for hydrolysis of Ap4A is 8.7% of that of the wild-type enzyme, KM-value is 6.7fold higher than the KM-value of the wild-type enzyme
Y76A/Y121A
-
turnover-number for hydrolysis of Ap4A is 4.8% of that of the wild-type enzyme, KM-value is 3.75fold higher than the KM-value of the wild-type enzyme
E58A
-
crystallization data
T70A
active site mutant, has no effect on platelet aggregation and secretion
E122Q
-
fusion protein containing and N-terminal extension Gly-Pro-Leu-Gly-Ser-Pro-Asn-Cys. KM-value is 20% of the wild-type value, turnover-number is 50% of the wild-type value. 2.3fold reduction in sensitivity to fluoride
E125Q
-
fusion protein containing and N-terminal extension Gly-Pro-Leu-Gly-Ser. KM-value is 0.7% of the wild-type value, turnover-number is 56% of the wild-type value. Cleavage of (2'-pdA)AppppA to produce ATP and 2'-deoxyadenylated AMP rather than 2'-deoxyadenylated ATP + AMP as with wild-type enzyme, the ratio of ATP released is increased compared to wild-type. 83fold reduction in sensitivity to fluoride
E55Q
-
fusion protein containing and N-terminal extension of Gly-Pro-Leu-Gly-Ser. KM-value is 4.8% of the wild-type value, turnover-number is 0.01% of the wild-type value. Activity with (2'-pdA)AppppA is to low to be detected. More than 330fold reduction in sensitivity to fluoride
E58D
-
fusion protein containing and N-terminal extension Gly-Pro-Leu-Gly-Ser-Pro-Asn-Cys. KM-value is 38.4% of the wild-type value, turnover-number is 9% of the wild-type value. Cleavage of (2'-pdA)AppppA to produce ATP and 2'-deoxyadenylated AMP rather than 2'-deoxyadenylated ATP + AMP as with wild-type enzyme, the ratio of ATP released is increased compared to wild-type. 16.7fold reduction in sensitivity to fluoride
E58Q
-
fusion protein containing and N-terminal extension Gly-Pro-Leu-Gly-Ser-Pro-Asn-Cys. KM-value is 80% of the wild-type value, turnover-number is 43.9% of the wild-type value. 6.7fold reduction in sensitivity to fluoride
E59D
-
fusion protein containing and N-terminal extension Gly-Pro-Leu-Gly-Ser-Pro-Asn-Cys. KM-value is 4fold higher than the wild-type value, turnover-number is 0.02% of the wild-type value. Activity with (2'-pdA)AppppA is to low to be detected. 2fold reduction in sensitivity to fluoride
E59Q
-
fusion protein containing and N-terminal extension Gly-Pro-Leu-Gly-Ser-Pro-Asn-Cys. KM-value is 2.4fold higher than the wild-type value, turnover-number is 0.00076% of the wild-type value. Activity with (2'-pdA)AppppA is to low to be detected
R54Q
-
fusion protein containing and N-terminal extension Gly-Pro-Leu-Gly-Ser-Pro-Asn-Cys. Cleavage of (2'-pdA)AppppA to produce ATP and 2'-deoxyadenylated AMP rather than 2'-deoxyadenylated ATP + AMP as with wild-type enzyme, the ratio of ATP released is increased compared to wild-type. 330fold reduction in sensitivity to fluoride
P133A
5fold increase in Km value
P133F
3fold decrease in kcat value
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