Any feedback?
Literature summary extracted from
- Reversal of the effect of the allosteric ligands of dCMP-aminohydrolase and stabilization of the enzyme in the T form (1982), J. Mol. Biol., 157, 557-570.
Activating Compound
| EC Number | Activating Compound | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.5.4.12 | ammonium sulfate | substrate dCMP-Hg-S-CH2-CH2-OH, 0.2 M ammonium sulfate: activation, reversed by cCTP | Equus asinus |  |
| 3.5.4.12 | dCTP | allosteric activator | Equus asinus | |
| 3.5.4.12 | dCTP | 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 | Equus asinus | |
| 3.5.4.12 | dTTP | 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 | Equus asinus | |
| 3.5.4.12 | Glutaraldehyde | substrate dCMP: rapid inhibition, protection by dGMP, or dTTP or both is slight, substrate dCMP-Hg-S-CH2-CH2-OH: 3fold activation | Equus asinus | |
| 3.5.4.12 | glycerol | substrate dCMP: activation, substrate dCMP-Hg-S-CH2-CH2-OH, 20% glycerol: inhibition | Equus asinus | |
General Stability
| EC Number | General Stability | Organism |
|---|---|---|
| 3.5.4.12 | dCTP or glycerol stabilize | Equus asinus |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.5.4.12 | 5-Hg-dCMP | irreversible competitive inhibitor, in the absence of mercaptoethanol | Equus asinus | |
| 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 | dCTP | 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 | Equus asinus | |
| 3.5.4.12 | dGMP | competitive inhibitor | Equus asinus | |
| 3.5.4.12 | dTTP | allosteric inhibitor; 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 | Equus asinus | |
| 3.5.4.12 | dUMP | competitive inhibitor | Equus asinus | |
| 3.5.4.12 | Glutaraldehyde | 25% glutaraldehyde: rapid inhibition; substrate dCMP: rapid inhibition, protection by dGMP, or dTTP or both is slight, substrate dCMP-Hg-S-CH2-CH2-OH: 3fold activation | Equus asinus | |
| 3.5.4.12 | glycerol | substrate dCMP: activation, substrate dCMP-Hg-S-CH2-CH2-OH, 20% glycerol: inhibition, removed by dTTP | 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 properties and parameters | Equus asinus | |
| 3.5.4.12 | additional information | - |
additional information | kinetic experiments | Equus asinus | |
| 3.5.4.12 | 0.26 | - |
dCMP-Hg-S-CH2-CH2-OH | - |
Equus asinus | |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 3.5.4.12 | 120000 | - |
- |
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 | catalyzed reaction is at a branching point of the pathway leading to dCTP and dTTP, immediate pyrimidine deoxynucleotide precursors in DNA biosynthesis | 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 | highly regulated allosteric enzyme | Equus asinus |
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 | 23 | - |
substrate: dCMP-Hg-S-CH2-CH2-OH | Equus asinus |
| 3.5.4.12 | 820 | - |
substrate: dCMP | Equus asinus |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.5.4.12 | 5-bromo-dCMP + H2O | - |
Equus asinus | 5-bromo-dUMP + NH3 | - |
? | |
| 3.5.4.12 | 5-fluoro-dCMP + H2O | - |
Equus asinus | 5-fluoro-dUMP + NH3 | - |
? | |
| 3.5.4.12 | 5-Hg-dCMP + H2O | deamination activated by dTTP and inhibited by dCTP | Equus asinus | 5-Hg-dUMP + NH3 | - |
? | |
| 3.5.4.12 | 5-Hg-dCMP + H2O | 5-mercury derivative of dCMP only in the presence of an excess of mercaptoethanol | Equus asinus | 5-Hg-dUMP + NH3 | - |
? | |
| 3.5.4.12 | 5-hydroxymethyl-dCMP + H2O | - |
Equus asinus | 5-hydroxymethyl-dUMP + NH3 | - |
? | |
| 3.5.4.12 | 5-iodo-dCMP + H2O | - |
Equus asinus | 5-iodo-dUMP + NH3 | - |
? | |
| 3.5.4.12 | 5-methyl-dCMP + H2O | - |
Equus asinus | 5-methyl-dUMP + NH3 | - |
? | |
| 3.5.4.12 | ara-CMP + H2O | arabinosyl-CMP | Equus asinus | ara-UMP + NH3 | - |
? | |
| 3.5.4.12 | ara-CMP + H2O | at a very low rate | Equus asinus | ara-UMP + NH3 | - |
? | |
| 3.5.4.12 | ara-CMP + H2O | effective substrate in presence of dCTP | Equus asinus | ara-UMP + NH3 | - |
? | |
| 3.5.4.12 | CMP + H2O | poor substrate | Equus asinus | UMP + NH3 | - |
? | |
| 3.5.4.12 | CMP + H2O | at a low rare, strongly activated by dCTP | Equus asinus | UMP + NH3 | - |
? | |
| 3.5.4.12 | dCMP + H2O | not a substrate of the T form, dTTP-induced form of the enzyme | Equus asinus | dUMP + NH3 | - |
? | |
| 3.5.4.12 | dCMP + H2O | catalyzed reaction is at a branching point of the pathway leading to dCTP and dTTP, immediate pyrimidine deoxynucleotide precursors in DNA biosynthesis | Equus asinus | dUMP + NH3 | - |
? | |
| 3.5.4.12 | dCMP-Hg-S-CH2-CH2-OH + H2O | better substrate of T form: in the presence of dTTP | Equus asinus | dUMP-Hg-S-CH2-CH2-OH + NH3 | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 3.5.4.12 | hexamer | 6 identical subunits | Equus asinus |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.5.4.12 | 38 | - |
assay at | Equus asinus |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.5.4.12 | 8 | - |
assay at, substrate: dCMP-Hg-S-CH2-CH2-OH | Equus asinus |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
