3.5.4.12: dCMP deaminase
This is an abbreviated version!
For detailed information about dCMP deaminase, go to the full flat file.
Word Map on EC 3.5.4.12
Reaction
Synonyms
2-deoxycytidylate deaminase, 5-mdCMP deaminase, 5-methyldeoxycytidine monophosphate deaminase, DCD, DCD1, dCDA, dCMP deaminase, dCMP-aminohydrolase, dCMP-dCTP deaminase, dCMPase, dCMPD, deaminase, deoxycytidylate, deoxy-CMP-deaminase, deoxycytidine deaminase, deoxycytidine monophosphate deaminase, deoxycytidine nucleotide deaminase, deoxycytidine-5'-monophosphate aminohydrolase, deoxycytidine-5'-monophosphate deaminase, deoxycytidine-5'-phosphate deaminase, deoxycytidylate aminohydrolase, deoxycytidylate deaminase, ST2 protein, STRIPE2, T2-dCMP deaminase, T2-deoxycytidylate deaminase, T2-phage deoxycytidylate deaminase, T4-dCMP deaminase, T4-deaminase, T4-phage deoxycytidylate deaminase
ECTree
3.5.4.12 dCMP deaminaseAdvanced search results
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results (Activating Compound
Activating Compound on EC 3.5.4.12 - dCMP deaminase
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ACTIVATING COMPOUND 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
(4Z,7Z,10Z,13Z,16Z,19Z)-henicosa-4,7,10,13,16,19-hexaenoic acid
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increases the enzyme activity in vivo in normal Rat-2 fibroblasts, but decreases it in transformed NM-16 fibroblasts
1-beta-D-arabinofuranosylcytosine 5'-triphosphate
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low activation, allosteric activator
3,4,5,6-tetrahydro-2'-dUMP
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high-affinity inhibitor, rapid, reversible inhibition, kinetics of inhibition. At low substrate or competitor concentrations: activation. Tetrahydro-dUMP activates enzyme at low substrate concentrations
ammonium sulfate
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substrate dCMP-Hg-S-CH2-CH2-OH, 0.2 M ammonium sulfate: activation, reversed by cCTP
deoxycytidine 5'-triphosphate
Tequatrovirus T4
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allosteric feedback regulation of the enzyme by products of the metabolic pathway, allosteric regulation involved residues 112 and 115
Glutaraldehyde
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substrate dCMP: rapid inhibition, protection by dGMP, or dTTP or both is slight, substrate dCMP-Hg-S-CH2-CH2-OH: 3fold activation
glycerol
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substrate dCMP: activation, substrate dCMP-Hg-S-CH2-CH2-OH, 20% glycerol: inhibition
pre-immune serum
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activation of host-cell enzyme, twice as effective as Herpes antiserum
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TTP
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activating enzyme up to 1.7fold at concentration of 0.00025 mM, but inhibiting at higher concentration, 0.015 mM: 85% inhibition
5-hydroxymethyl-dCTP
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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
5-hydroxymethyl-dCTP
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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
5-hydroxymethyl-dCTP
Tequatrovirus T4
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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
dAMP
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competitive inhibitor, activates enzyme at low substrate concentration mimicing the cooperative effect of the substrate, dAMP activates dCMPase 4fold at low substrate concentration, no activating effect on the modified enzyme, glutaraldehyde-dCMPase
dAMP
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at low substrate, dCMP, concentration: activation at higher concentration of either: inhibition
dCTP
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maximum activation at 0.04 mM, dCTP activation requires presence of Mg2+ or Mn2+
dCTP
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enzyme from Herpes simplex virus infected BHK-21/C13 cells from baby-hamster: maximum activation is achieved by lower concentration of dCTP than of enzyme from non-infected cells
dCTP
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allosteric activator, 12fold, for aminohydrolysis of dCMP, inhibitor, 50% inhibition, for substrate: 5-Hg-dCMP in the presence of mercaptoethanol, dCMP-Hg-S-CH2-CH2-OH
dCTP
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glutaraldehyde fixes dCMPase in the activated conformation induced by dCTP
dCTP
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positive allosteric effector
dCTP
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activation by dCTP decreases markedly as the pH is increased, pH-dependent activation
dCTP
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dCTP promotes an aggregation of enzyme subunits to the active state
dCTP
Herpes simplex virus
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enzyme from Herpes simplex virus infected BHK-21/C13 cells from baby-hamster: maximum activation is achieved by lower concentration of dCTP than of enzyme from non-infected cells
dCTP
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activation by dCTP has absolute requirement for the presence of a divalent cation, Mg2+, Ca2+ and Mn2+ are equally effective cations for enzyme activation by dCTP
dCTP
activates dCMP deamination about 7fold at 0.005-0.1 mM
dCTP
Tequatrovirus T4
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hexameric form of enzyme is activated by dCTP, while the dimer is not
dCTP
Tequatrovirus T4
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wild-type, dCTP required for activity, no activity in absence of dCTP and Mg2+
dCTP
Tequatrovirus T4
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mutants R115E and R115Q: dCTP not required. R115Q: slight, 30-40% activation by 0.02 mM dCTP
dTTP
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allosteric inhibitor, 100% inhibition, for substrate dCMP, becomes activator, 2.5fold, for mercury substrate: 5-Hg-dCMP in the presence of mercaptoethanol, dCMP-Hg-S-CH2-CH2-OH, at relatively high, 1 to 2 mM, dCMP-Hg-S-CH2-CH2-OH concentration
dTTP
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allosteric inhibitor, 100% inhibition, for substrate dCMP, becomes activator, 2.5fold, for mercury substrate: 5-Hg-dCMP in the presence of mercaptoethanol, dCMP-Hg-S-CH2-CH2-OH, at relatively high, 1 to 2 mM, dCMP-Hg-S-CH2-CH2-OH concentration
additional information
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infection with the human cytomegalovirus upregulates the enzyme involved in thymidylate synthesis especially the dCMP deaminase, but not the dUTPase, overview
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additional information
Tequatrovirus T4
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the phage dCMP deaminase expression is increased upon infection of Escherichia coli
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