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Literature summary for 3.5.4.12 extracted from

  • Maley, G.F.; Guarino, D.U.
    T2r+ bacteriophage-induced enzymes. I. The purification and properties of deoxycytidylate deaminase (1972), J. Biol. Chem., 247, 931-939.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
5-hydroxymethyl-dCTP natural positive allosteric effector, enzyme is much more effectively regulated by its natural effector, 5-hydroxymethyl-dCTP, than by dCTP, binding of 5-hydroxymethyl-dCTP is much more pH dependent than dCTP Tequatrovirus T4
5-hydroxymethyl-dCTP natural positive allosteric effector, enzyme is much more effectively regulated by its natural effector, 5-hydroxymethyl-dCTP, than by dCTP, binding of 5-hydroxymethyl-dCTP is much more pH dependent than dCTP Escherichia phage T2
5-hydroxymethyl-dCTP pH-dependent activation Tequatrovirus T4
5-hydroxymethyl-dCTP pH-dependent activation Escherichia phage T2
dCTP positive allosteric effector Gallus gallus
dCTP positive allosteric effector Tequatrovirus T4
dCTP positive allosteric effector Escherichia phage T2
dCTP activation by dCTP decreases markedly as the pH is increased, pH-dependent activation Escherichia phage T2

General Stability

General Stability Organism
2-mercaptoethanol stabilizes Tequatrovirus T4
2-mercaptoethanol stabilizes Escherichia phage T2

Inhibitors

Inhibitors Comment Organism Structure
dTTP allosteric inhibitor; inhibition by dTTP increases markedly as the pH is raised, pH-dependent inhibition Escherichia phage T2
dTTP allosteric inhibitor Gallus gallus
dTTP allosteric inhibitor Tequatrovirus T4

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.05
-
dCMP pH 6.0 Escherichia phage T2
0.1
-
dCMP pH 8.0 Escherichia phage T2
0.5
-
CMP pH 6.0 Escherichia phage T2
12
-
CMP pH 8.0, absence of effector Escherichia phage T2

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
124000
-
PAGE and sedimentation equilibrium Escherichia phage T2

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
dCMP + H2O Gallus gallus major function to provide supplementary route for dTMP synthesis, located at a branch point in pyrimidine metabolic pathway dUMP + NH3
-
?
dCMP + H2O Tequatrovirus T4 major function to provide supplementary route for dTMP synthesis, located at a branch point in pyrimidine metabolic pathway dUMP + NH3
-
?
dCMP + H2O Escherichia phage T2 major function to provide supplementary route for dTMP synthesis, located at a branch point in pyrimidine metabolic pathway dUMP + NH3
-
?

Organism

Organism UniProt Comment Textmining
Escherichia phage T2
-
T2r+ or T4r+ bacteriophage-induced enzyme, host Escherichia coli B
-
Gallus gallus
-
-
-
Tequatrovirus T4
-
T2r+ or T4r+ bacteriophage-induced enzyme, host Escherichia coli B
-

Purification (Commentary)

Purification (Comment) Organism
T2-phage infected Escherichia coli Escherichia phage T2
T4-phage infected Escherichia coli Tequatrovirus T4

Reaction

Reaction Comment Organism Reaction ID
dCMP + H2O = dUMP + NH3 regulation, allosteric end-product regulation Gallus gallus
dCMP + H2O = dUMP + NH3 regulation, allosteric end-product regulation Tequatrovirus T4
dCMP + H2O = dUMP + NH3 regulation, allosteric end-product regulation Escherichia phage T2
dCMP + H2O = dUMP + NH3 feedback regulation Gallus gallus
dCMP + H2O = dUMP + NH3 feedback regulation Tequatrovirus T4
dCMP + H2O = dUMP + NH3 feedback regulation Escherichia phage T2
dCMP + H2O = dUMP + NH3 highly regulated allosteric enzyme Gallus gallus
dCMP + H2O = dUMP + NH3 highly regulated allosteric enzyme Tequatrovirus T4
dCMP + H2O = dUMP + NH3 highly regulated allosteric enzyme Escherichia phage T2

Source Tissue

Source Tissue Comment Organism Textmining
embryo
-
Gallus gallus
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
430
-
-
Escherichia phage T2

Storage Stability

Storage Stability Organism
0-4°C, neutral pH, 0.1 M 2-mercaptoethanol, stable for several months Escherichia phage T2
frozen in absence of 2-mercaptoethanol, indefinitely stable Escherichia phage T2

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5-hydroxymethyl-dCMP + H2O
-
Gallus gallus 5-hydroxymethyl-dUMP + NH3
-
?
5-hydroxymethyl-dCMP + H2O very poor substrate Tequatrovirus T4 5-hydroxymethyl-dUMP + NH3
-
?
5-hydroxymethyl-dCMP + H2O very poor substrate Escherichia phage T2 5-hydroxymethyl-dUMP + NH3
-
?
CMP + H2O
-
Tequatrovirus T4 UMP + NH3
-
?
CMP + H2O
-
Escherichia phage T2 UMP + NH3
-
?
dCMP + H2O
-
Gallus gallus dUMP + NH3
-
?
dCMP + H2O
-
Tequatrovirus T4 dUMP + NH3
-
?
dCMP + H2O
-
Escherichia phage T2 dUMP + NH3
-
?
dCMP + H2O major function to provide supplementary route for dTMP synthesis, located at a branch point in pyrimidine metabolic pathway Gallus gallus dUMP + NH3
-
?
dCMP + H2O major function to provide supplementary route for dTMP synthesis, located at a branch point in pyrimidine metabolic pathway Tequatrovirus T4 dUMP + NH3
-
?
dCMP + H2O major function to provide supplementary route for dTMP synthesis, located at a branch point in pyrimidine metabolic pathway Escherichia phage T2 dUMP + NH3
-
?

Subunits

Subunits Comment Organism
hexamer 6 identical subunits Gallus gallus
hexamer 6 identical subunits Tequatrovirus T4
hexamer 6 identical subunits Escherichia phage T2

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Tequatrovirus T4
37
-
assay at Escherichia phage T2

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
additional information
-
dCTP increases pH-optimum by approximately 3 pH units Escherichia phage T2
additional information
-
dCTP increases pH-optimum by approximately 0.6 unit Gallus gallus
5.3
-
in the absence of dCTP Escherichia phage T2
8.3
-
in the presence of dCTP or 5-hydroxymethyl-dCTP Escherichia phage T2