Information on EC 3.1.5.B1 - dNTPase

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

EC NUMBER
COMMENTARY hide
3.1.5.B1
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
dNTPase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
dNTP + H2O = a deoxynucleotide + triphosphate
show the reaction diagram
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-
-
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SYSTEMATIC NAME
IUBMB Comments
dNTP triphosphorylase
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
dATP + H2O
deoxyadenosine + triphosphate
show the reaction diagram
dCTP + H2O
deoxycytidine + triphosphate
show the reaction diagram
dGTP + H2O
deoxyguanosine + triphosphate
show the reaction diagram
dTTP + H2O
deoxythymidine + triphosphate
show the reaction diagram
additional information
?
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
dATP
both dATP and dGTP are co-activators for hydrolysis of dTTP, dATP might bind at the secondary allosteric site
dCTP
allosteric activator, less potent than dGTP and dATP
additional information
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.22 - 0.34
dATP
0.2 - 0.29
dCTP
0.22 - 0.24
dGTP
0.28 - 0.3
dTTP
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1 - 4.4
dATP
0.9 - 2.2
dCTP
0.9 - 2.9
dGTP
1 - 4.1
dTTP
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
72000
-
and 280000, gel filtration
72600
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1 * 72600, and tetramer, 4 * 72600, analytical ultracentrifugation. Formation of tetramer is induced by dGTP, tetramer is a more potent dNTPase than monomer; 4 * 72600, and monomer, 1 * 72600, analytical ultracentrifugation. Formation of tetramer is induced by dGTP, tetramer is a more potent dNTPase than monomer
280000
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and 72000, gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
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1 * 72600, and tetramer, 4 * 72600, analytical ultracentrifugation. Formation of tetramer is induced by dGTP, tetramer is a more potent dNTPase than monomer
tetramer
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4 * 72600, and monomer, 1 * 72600, analytical ultracentrifugation. Formation of tetramer is induced by dGTP, tetramer is a more potent dNTPase than monomer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystal structure in complex with dGTP and dTTP, to 2.35 A resolution. The tetrameric enzyme EF1143 contains four additional secondary allosteric sites adjacent to the previously identified dGTP-binding primary regulatory sites. dGTP binding to the first allosteric site, with nanomolar affinity, is a prerequisite for substrate docking and hydrolysis. Then, the presence of a particular dNTP in the second site either enhances or inhibits the dNTPase activity
in complex with the allosteric activator and substrate dGTP/dATP, to 1.8 A resolution
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
enzyme is variably expressed during the cell cycle, maximally during quiescence and minimally during S-phase
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maximum expression in quiescent cells
maximum expressionin quescent cells
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H114A
no residual activity
H129A
less than 5% residual activity
K14A
less than 5% residual activity
K330A
no residual activity
N36A
no residual activity
Q241A
about 10% residual activity
Q41A
less than 5% residual activity
R17A
no residual activity
R17Q
about 5% residual activity
R206A/R209A
no residual activity
R206Q
about 30% residual activity
R209S
about 70% residual activity
R326A
about 40% residual activity
Y199A
no residual activity
H114A
-
no residual activity
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H129A
-
less than 5% residual activity
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K14A
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less than 5% residual activity
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R17A
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no residual activity
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Y199A
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no residual activity
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D137A
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reduced ability to form tetramers, reduced dNTPase activity
Q142E/R145K
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reduced ability to form tetramers, reduced dNTPase activity
R333E
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reduced ability to form tetramers, reduced dNTPase activity
R333E/R451E
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reduced ability to form tetramers, reduced dNTPase activity
R451E
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reduced ability to form tetramers, reduced dNTPase activity