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Literature summary for 3.5.4.12 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

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

Inhibitors

Inhibitors Comment Organism Structure
dAMP competitive inhibitor, activates enzyme at low substrate concentration mimicing the cooperative effect of the substrate Equus asinus
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
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]

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

Metals/Ions

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

Molecular Weight [Da]

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Equus asinus
-
donkey
-
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)

Purification (Comment) Organism
-
Equus asinus

Reaction

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

Source Tissue

Source Tissue Comment Organism Textmining
spleen
-
Equus asinus
-

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

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

Subunits

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

Temperature Optimum [°C]

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

pH Optimum

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