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Literature summary extracted from
- Crystal structures of Streptococcus mutans 2-deoxycytidylate deaminase and its complex with substrate analog and allosteric regulator dCTP x Mg2+ (2008), J. Mol. Biol., 377, 220-231.
Activating Compound
| EC Number | Activating Compound | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.5.4.12 | dCTP | an allosteric activator, in complex with Mg2+ | Streptococcus mutans |  |
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 3.5.4.12 | overexpression of His-tagged enzyme in Escherichia coli strain BL21(DE3) | Streptococcus mutans |
Crystallization (Commentary)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 3.5.4.12 | dCMP deaminase in complex with dCTP and an intermediate analogue, X-ray diffraction structure determination and analysis at 1.66-3.0 A resolution, the crystal structure of the free-state enzyme is determined by the zinc multiwavelength anomalous dispersion, MAD, method | Streptococcus mutans |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.5.4.12 | dTTP | an allosteric inhibitor | Streptococcus mutans | |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.5.4.12 | Ca2+ | can partially substitute for Mg2+, 50% of the activity with Mg2+ | Streptococcus mutans | |
| 3.5.4.12 | Mg2+ | required for activity, in complex with activator dCTP, can be substituted by Ca2+ or Mn2+, but not by Zn2+, Co2+, Ni2+, and Cu2+ | Streptococcus mutans | |
| 3.5.4.12 | Mn2+ | can partially substitute for Mg2+, 26% of the activity with Mg2+ | Streptococcus mutans | |
| 3.5.4.12 | additional information | Co2+, Ni2+, and Cu2+ cannot substitute for Mg2+ | Streptococcus mutans | |
| 3.5.4.12 | Zn2+ | two conserved motifs are involved in the binding of Zn2+, Zn2+ cannot substitute for Mg2+ | Streptococcus mutans | |
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 | Streptococcus mutans | the regulation signal is transmitted by Arg4 from the allosteric site to the active site via modifications in the interactions at the interface where the substrate binding pocket is involved and the relocations of Arg26, His65, Tyr120, and Arg121 to envelope the active site in order to stabilize substrate binding in the complex, allosteric mechanism for enzyme regulation, regulator binding structure, overview | dUMP + NH3 | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.5.4.12 | Streptococcus mutans | - |
- |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 3.5.4.12 | recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration | Streptococcus mutans |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.5.4.12 | dCMP + H2O | the regulation signal is transmitted by Arg4 from the allosteric site to the active site via modifications in the interactions at the interface where the substrate binding pocket is involved and the relocations of Arg26, His65, Tyr120, and Arg121 to envelope the active site in order to stabilize substrate binding in the complex, allosteric mechanism for enzyme regulation, regulator binding structure, overview | Streptococcus mutans | dUMP + NH3 | - |
? | |
| 3.5.4.12 | dCMP + H2O | a conserved motif, G43YNG46, is involved in the binding of dCTP, N-terminal Arg4, a key residue located between two monomers, binds strongly to the gamma phosphate group of dCTP, active site structure and substrate binding, overview | Streptococcus mutans | dUMP + NH3 | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 3.5.4.12 | hexamer | homohexamer, subunits adopt a three-layer alpha/beta/alpha sandwich fold | Streptococcus mutans |
| 3.5.4.12 | More | monomeric and quarternary structure analysis, overview | Streptococcus mutans |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.5.4.12 | 2-deoxycytidylate deaminase | - |
Streptococcus mutans |
| 3.5.4.12 | deoxycytidine-5'-monophosphate deaminase | - |
Streptococcus mutans |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.5.4.12 | 30 | - |
assay at | Streptococcus mutans |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.5.4.12 | 8 | - |
assay at | Streptococcus mutans |
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