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 | Escherichia phage T2 | |
5-hydroxymethyl-dCTP | pH-dependent activation | Escherichia phage T2 | |
dCTP | pH-dependent activation | Gallus gallus | |
dCTP | positive allosteric effector | Gallus gallus | |
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 | Organism |
---|---|
2-mercaptoethanol stabilizes | Escherichia phage T2 |
guanidine hydrochloride, 1 M, complete loss in activity accompanied by disaggregation of enzyme, 6 M: denaturation, complete reactivation with 50 mM 2-mercaptoethanol | Escherichia phage T2 |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
dTTP | allosteric inhibitor | Escherichia phage T2 | |
dTTP | allosteric inhibitor | Gallus gallus | |
guanidine hydrochloride | 0.5 M: 50% inhibition, 1 M: 100% inhibition | Escherichia phage T2 |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
20200 | - |
6 * 20200, sedimentation in 6 M guanidine hydrochloride containing 0.1 M 2-mercaptoethanol and SDS-PAGE | Escherichia phage T2 |
124000 | - |
PAGE and sedimentation equilibrium | Escherichia phage T2 |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
dCMP + H2O | Gallus gallus | - |
dUMP + NH3 | - |
? | |
dCMP + H2O | Escherichia phage T2 | - |
dUMP + NH3 | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia phage T2 | - |
T2r+-infected Escherichia coli B | - |
Gallus gallus | - |
- |
- |
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 | Escherichia phage T2 | |
dCMP + H2O = dUMP + NH3 | highly regulated allosteric enzyme | Gallus gallus | |
dCMP + H2O = dUMP + NH3 | highly regulated allosteric enzyme | Escherichia phage T2 |
Renatured (Comment) | Organism |
---|---|
after treatment with guanidine hydrochloride, 6 M, complete reactivation with 50 mM 2-mercaptoethanol, original hexameric structure restored | Escherichia phage T2 |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
embryo | - |
Gallus gallus | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
dCMP + H2O | - |
Gallus gallus | dUMP + NH3 | - |
? | |
dCMP + H2O | - |
Escherichia phage T2 | dUMP + NH3 | - |
? |
Subunits | Comment | Organism |
---|---|---|
hexamer | 6 identical subunits | Gallus gallus |
hexamer | 6 identical subunits | Escherichia phage T2 |
hexamer | hexamer is the active form | Escherichia phage T2 |
hexamer | 6 * 20200, sedimentation in 6 M guanidine hydrochloride containing 0.1 M 2-mercaptoethanol and SDS-PAGE | Escherichia phage T2 |