3.1.5.B1: dNTPase
This is an abbreviated version!
For detailed information about dNTPase, go to the full flat file.
Word Map on EC 3.1.5.B1
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3.1.5.B1
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myeloid
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dntps
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domain-containing
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viruses
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dendritic
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lentiviruses
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retroviral
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simian
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retroviruses
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deoxynucleotide
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histidine-aspartate
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monocyte-derived
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vpx-mediated
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vpr
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antiretroviral
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deoxyribonucleoside
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sivmac
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apobec3g
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non-cycling
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non-dividing
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anti-hiv-1
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tetherin
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chilblain
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line-1
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aicardi-goutieres
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rnaseh2a
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interferon-stimulated
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retrotransposition
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interferonopathy
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cytarabine
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sivsm
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mddcs
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medicine
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analysis
- 3.1.5.B1
- myeloid
- dntps
-
domain-containing
- viruses
- dendritic
- lentiviruses
-
retroviral
-
simian
- retroviruses
- deoxynucleotide
-
histidine-aspartate
-
monocyte-derived
-
vpx-mediated
- vpr
-
antiretroviral
- deoxyribonucleoside
-
sivmac
- apobec3g
-
non-cycling
-
non-dividing
-
anti-hiv-1
-
tetherin
-
chilblain
-
line-1
-
aicardi-goutieres
- rnaseh2a
-
interferon-stimulated
-
retrotransposition
-
interferonopathy
- cytarabine
-
sivsm
-
mddcs
- medicine
- analysis
Reaction
Synonyms
deoxynucleoside triphosphate triphosphohydrolase, deoxyribonucleotide triphosphohydrolase, EF_1143, HD domain protein, SAMHD1
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3.1.5.B1 dNTPaseAdvanced search results
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results (Activating Compound
Activating Compound on EC 3.1.5.B1 - dNTPase
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ACTIVATING COMPOUND 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
dATP
both dATP and dGTP are co-activators for hydrolysis of dTTP, dATP might bind at the secondary allosteric site
dNTP
both GTP and dNTP are required for tetramer activation of the enzyme. SAMHD1 activation is regulated by the concentration of dNTP
dGTP
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
dGTP
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allosteric activator. Allosteric dGTP binding induces conformational changes at the active site, allowing a more stable interaction with the substrate and explaining the dGTP-induced isoform SAMHD1 dNTPase activity. Mutations of dGTP binding residues in the allosteric site affect tetramer formation, dNTPase activity and HIV-1 restriction
dGTP
low concentrations of either GTP or dGTP stimulate the reaction maximally, Km value for binding to allosteric site 1 is 0.00015 mM with substrate dATP
dGTP
low concentrations of either GTP or dGTP stimulate the reaction maximally, Km value for binding to allosteric site 1 is 0.0008 mM with substrate dATP
dGTP
dGTP causes ISF1 to tetramerize, activating its catalytic activity. Isoform ISF2 has dGTP-independent catalytic activity
GTP
low concentrations of either GTP or dGTP stimulate the reaction maximally, Km value for binding to allosteric site 1 is 0.00015 mM with substrate dATP. In quiescent cells where the enzyme is maximally expressed GTP binds to allosteric site 1 with very high affinity, stabilizing site 2 of the tetrameric structure. Any canonical dNTP can bind to site 2 and activate the enzyme, but in cells only dATP or dTTP are present at sufficient concentrations. Tetrameric enzyme is activated for the hydrolysis of any dNTP only after binding of a dNTP to site 2
GTP
low concentrations of either GTP or dGTP stimulate the reaction maximally, Km value for binding to allosteric site 1 is 0.0005 mM with substrate dATP. In quiescent cells where the enzyme is maximally expressed GTP binds to allosteric site 1 with very high affinity, stabilizing site 2 of the tetrameric structure. Any canonical dNTP can bind to site 2 and activate the enzyme, but in cells only dATP or dTTP are present at sufficient concentrations. Tetrameric enzyme is activated for the hydrolysis of any dNTP only after binding of a dNTP to site 2
additional information
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dGTP, but not the other dNTPs, is required for the formation and maintenance of the catalytically more active SAMHD1 tetramer
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additional information
in quiescent cells where the enzyme is maximally expressed GTP binds to allosteric site 1 with very high affinity, stabilizing site 2 of the tetrameric structure. Any canonical dNTP can bind to site 2 and activate the enzyme, but in cells only dATP or dTTP are present at sufficient concentrations. Tetrameric enzyme is activated for the hydrolysis of any dNTP only after binding of a dNTP to site 2
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additional information
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in quiescent cells where the enzyme is maximally expressed GTP binds to allosteric site 1 with very high affinity, stabilizing site 2 of the tetrameric structure. Any canonical dNTP can bind to site 2 and activate the enzyme, but in cells only dATP or dTTP are present at sufficient concentrations. Tetrameric enzyme is activated for the hydrolysis of any dNTP only after binding of a dNTP to site 2
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additional information
in quiescent cells where the enzyme is maximally expressed GTP binds to allosteric site 1 with very high affinity, stabilizing site 2 of the tetrameric structure. Any canonical dNTP can bind to site 2 and activate the enzyme, but in cells only dATP or dTTP are present at sufficient concentrations. Tetrameric enzyme is activated for the hydrolysis of any dNTP only after binding of a dNTP to site 2
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additional information
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in quiescent cells where the enzyme is maximally expressed GTP binds to allosteric site 1 with very high affinity, stabilizing site 2 of the tetrameric structure. Any canonical dNTP can bind to site 2 and activate the enzyme, but in cells only dATP or dTTP are present at sufficient concentrations. Tetrameric enzyme is activated for the hydrolysis of any dNTP only after binding of a dNTP to site 2
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