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Literature summary extracted from

  • Miazzi, C.; Ferraro, P.; Pontarin, G.; Rampazzo, C.; Reichard, P.; Bianchi, V.
    Allosteric regulation of the human and mouse deoxyribonucleotide triphosphohydrolase sterile alpha-motif/histidine-aspartate domain-containing protein 1 (SAMHD1) (2014), J. Biol. Chem., 289, 18339-18346.
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.1.5.B1 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 Homo sapiens
3.1.5.B1 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 Mus musculus
3.1.5.B1 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 Homo sapiens
3.1.5.B1 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 Mus musculus
3.1.5.B1 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 Homo sapiens
3.1.5.B1 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 Mus musculus

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.5.B1 expression in Escherichia coli Homo sapiens
3.1.5.B1 expression in Escherichia coli Mus musculus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.1.5.B1 0.2
-
 dCTP pH 7.5, 37°C, presence of 0.02 mM GTP plus 0.02 mM dATP Mus musculus
3.1.5.B1 0.22
-
 dGTP pH 7.5, 37°C Mus musculus
3.1.5.B1 0.22
-
 dATP pH 7.5, 37°C, presence of 0.02 mM GTP Mus musculus
3.1.5.B1 0.24
-
 dGTP pH 7.5, 37°C Homo sapiens
3.1.5.B1 0.28
-
 dTTP pH 7.5, 37°C, presence of 0.02 mM GTP plus 0.02 mM dATP Mus musculus
3.1.5.B1 0.29
-
 dCTP pH 7.5, 37°C, presence of 0.02 mM GTP plus 0.02 mM dATP Homo sapiens
3.1.5.B1 0.3
-
 dTTP pH 7.5, 37°C, presence of 0.02 mM GTP plus 0.02 mM dATP Homo sapiens
3.1.5.B1 0.34
-
 dATP pH 7.5, 37°C, presence of 0.02 mM GTP Homo sapiens

Organism

EC Number Organism UniProt Comment Textmining
3.1.5.B1 Homo sapiens Q9Y3Z3
-
-
3.1.5.B1 Mus musculus Q60710
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.5.B1 dATP + H2O
-
 Homo sapiens deoxyadenosine + triphosphate
-
 ?
3.1.5.B1 dATP + H2O
-
 Mus musculus deoxyadenosine + triphosphate
-
 ?
3.1.5.B1 dCTP + H2O
-
 Homo sapiens deoxycytidine + triphosphate
-
 ?
3.1.5.B1 dCTP + H2O
-
 Mus musculus deoxycytidine + triphosphate
-
 ?
3.1.5.B1 dGTP + H2O
-
 Homo sapiens deoxyguanosine + triphosphate
-
 ?
3.1.5.B1 dGTP + H2O
-
 Mus musculus deoxyguanosine + triphosphate
-
 ?
3.1.5.B1 dTTP + H2O
-
 Homo sapiens deoxythymidine + triphosphate
-
 ?
3.1.5.B1 dTTP + H2O
-
 Mus musculus deoxythymidine + triphosphate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.1.5.B1 deoxyribonucleotide triphosphohydrolase
-
 Homo sapiens
3.1.5.B1 deoxyribonucleotide triphosphohydrolase
-
 Mus musculus

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.1.5.B1 0.9
-
 dGTP pH 7.5, 37°C Homo sapiens
3.1.5.B1 0.9
-
 dCTP pH 7.5, 37°C, presence of 0.02 mM GTP plus 0.02 mM dATP Homo sapiens
3.1.5.B1 1
-
 dATP pH 7.5, 37°C, presence of 0.02 mM GTP Homo sapiens
3.1.5.B1 1
-
 dTTP pH 7.5, 37°C, presence of 0.02 mM GTP plus 0.02 mM dATP Homo sapiens
3.1.5.B1 2.2
-
 dCTP pH 7.5, 37°C, presence of 0.02 mM GTP plus 0.02 mM dATP Mus musculus
3.1.5.B1 2.9
-
 dGTP pH 7.5, 37°C Mus musculus
3.1.5.B1 4.1
-
 dTTP pH 7.5, 37°C, presence of 0.02 mM GTP plus 0.02 mM dATP Mus musculus
3.1.5.B1 4.4
-
 dATP pH 7.5, 37°C, presence of 0.02 mM GTP Mus musculus

Expression

EC Number Organism Comment Expression
3.1.5.B1 Mus musculus maximum expression in quiescent cells additional information
3.1.5.B1 Homo sapiens maximum expressionin quescent cells additional information