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Literature summary extracted from

  • Nucci, R.; Raia, C.A.; Vaccaro, C.; Sepe, S.; Scarano, E.; Rossi, M.
    Freezing of dCMP aminohydrolase in the activated conformation by glutaraldehyde (1978), J. Mol. Biol., 124, 133-145.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.5.4.12 dAMP 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 Equus asinus
3.5.4.12 dCTP allosteric activator Equus asinus
3.5.4.12 dCTP activate form: dCTP-enzyme Equus asinus
3.5.4.12 dCTP glutaraldehyde fixes dCMPase in the activated conformation induced by dCTP Equus asinus
3.5.4.12 dCTP dCMPase is activated 15.3fold, glutaraldehyde-dCMPase only 1.8fold Equus asinus

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.5.4.12 dAMP competitive inhibitor, activates enzyme at low substrate concentration mimicing the cooperative effect of the substrate Equus asinus
3.5.4.12 dTTP 0.01 mM: 100% inhibition. In the presence of glutaraldehyde enzyme is less sensitive to inhibitory effect of dTTP; allosteric inhibitor; inhibited form: dTTP-enzyme; kinetics of inhibition Equus asinus
3.5.4.12 Glutaraldehyde 25% glutaraldehyde: rapid inhibition; dCTP protects enzyme to a certain extent. Glutaraldehyde fixes dCMPase in the activated conformation induced by dCTP Equus asinus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.5.4.12 additional information
-
 additional information kinetic experiments Equus asinus
3.5.4.12 additional information
-
 additional information Km-value of modified enzyme, glutaraldehyde-dCMPase, is lower than that of native enzyme Equus asinus
3.5.4.12 additional information
-
 additional information kinetic data, kinetics typical of activated enzyme Equus asinus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.5.4.12 Mg2+ required for activation by dCTP and for inhibition by dTTP Equus asinus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.5.4.12 20000
-
 6 * 20000, SDS-PAGE Equus asinus
3.5.4.12 120000
-
 PAGE Equus asinus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.5.4.12 dCMP + H2O Equus asinus
-
 dUMP + NH3
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.5.4.12 Equus asinus
-
 donkey
-
3.5.4.12 Equus asinus
-
 three conformational isomers of dCMPase, the conformation of the enzyme with no ligands, the activated form, R form: dCTP-Mg complex and the inhibited form, T form: dTTP-Mg complex
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.5.4.12
-
 Equus asinus

Reaction

EC Number Reaction Comment Organism Reaction ID
3.5.4.12 dCMP + H2O = dUMP + NH3 regulation, allosteric end-product regulation Equus asinus
a
3.5.4.12 dCMP + H2O = dUMP + NH3 highly regulated allosteric enzyme Equus asinus
a

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.5.4.12 spleen
-
 Equus asinus
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.5.4.12 additional information
-
-
 Equus asinus
3.5.4.12 720
-
-
 Equus asinus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.4.12 5-methyl-dCMP + H2O
-
 Equus asinus 5-methyl-dUMP + NH3
-
 ?
3.5.4.12 ara-CMP + H2O deaminated only in the presence of dCTP, strongly activated by dCTP Equus asinus ara-UMP + NH3
-
 ?
3.5.4.12 ara-CMP + H2O arabinosyl-CMP Equus asinus ara-UMP + NH3
-
 ?
3.5.4.12 CMP + H2O deaminated only in the presence of dCTP, strongly activated by dCTP Equus asinus UMP + NH3
-
 ?
3.5.4.12 dCMP + H2O
-
 Equus asinus dUMP + NH3
-
 ?
3.5.4.12 additional information substrate specificity Equus asinus ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.5.4.12 hexamer 6 identical subunits Equus asinus
3.5.4.12 hexamer 6 * 20000, SDS-PAGE Equus asinus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.5.4.12 37
-
 assay at Equus asinus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.5.4.12 7.5
-
 assay at Equus asinus