Literature summary extracted from
Almog, R.; Maley, F.; Maley, G.F.; Maccoll, R.; Van Roey, P.
Three-dimensional structure of the R115E mutant of T4-bacteriophage 2-deoxycytidylate deaminase (2004), Biochemistry, 43, 13715-13723.
Activating Compound
EC Number |
Activating Compound |
Comment |
Organism |
Structure |
---|
3.5.4.12 |
deoxycytidine 5'-triphosphate |
allosteric feedback regulation of the enzyme by products of the metabolic pathway, allosteric regulation involved residues 112 and 115 |
Tequatrovirus T4 |
|
Application
EC Number |
Application |
Comment |
Organism |
---|
3.5.4.12 |
medicine |
the enzyme is a major target for cancer chemotherapy |
Tequatrovirus T4 |
Cloned(Commentary)
EC Number |
Cloned (Comment) |
Organism |
---|
3.5.4.12 |
expression of mutant R115E in Escherichia coli |
Tequatrovirus T4 |
Crystallization (Commentary)
EC Number |
Crystallization (Comment) |
Organism |
---|
3.5.4.12 |
purified mutant R115E free or in complex with active site binding inhibitor pyrimidin-2-one deoxyribotide, the mutant R115E is dimeric in solution, while hexameric in crystals, hanging drop vapour diffusion method, 0.28 mM mutant R115E protein in 20 mM phosphate, pH 7.2, 0.38 mM inhibitor, and 30 mM DTT, is mixed with an equal volume of reservoir solution containing 1.3 M ammonium sulfate, 0.1 M sodium citrate, pH 6.0, and 10 mM DTT, 22°C, 3 weeks, X-ray diffraction structure determination and analysis at 2.2 A resolution |
Tequatrovirus T4 |
Protein Variants
EC Number |
Protein Variants |
Comment |
Organism |
---|
3.5.4.12 |
R115E |
site-directed mutagenesis, quarternary structure analysis |
Tequatrovirus T4 |
Inhibitors
EC Number |
Inhibitors |
Comment |
Organism |
Structure |
---|
3.5.4.12 |
deoxythymidine 5'-triphosphate |
allosteric feedback regulation of the enzyme by products of the metabolic pathway, allosteric regulation involved residues 112 and 115 |
Tequatrovirus T4 |
|
3.5.4.12 |
pyrimidin-2-one deoxyribotide |
active site binding structure, overview |
Tequatrovirus T4 |
|
Metals/Ions
EC Number |
Metals/Ions |
Comment |
Organism |
Structure |
---|
3.5.4.12 |
Zn2+ |
the enzyme shows a zinc ion-based reaction mechanism, binding structure and coordinating residues, two zinc ions per subunit, the first is coordinated by His104, Cys132, and Cys135, the second by Cys19, Cys49, His94, and Glu102, overview |
Tequatrovirus T4 |
|
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 |
Tequatrovirus T4 |
the enzyme is the major supplier of substrate for the thymidylate synthase important in DNA synthesis |
dUMP + NH3 |
- |
? |
|
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
3.5.4.12 |
Tequatrovirus T4 |
- |
- |
- |
Purification (Commentary)
EC Number |
Purification (Comment) |
Organism |
---|
3.5.4.12 |
recombinant mutant R115E from Escherichia coli |
Tequatrovirus T4 |
Reaction
EC Number |
Reaction |
Comment |
Organism |
Reaction ID |
---|
3.5.4.12 |
dCMP + H2O = dUMP + NH3 |
zinc ion-based reaction mechanism, substrate binding structure |
Tequatrovirus T4 |
|
Substrates and Products (Substrate)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
3.5.4.12 |
dCMP + H2O |
- |
Tequatrovirus T4 |
dUMP + NH3 |
- |
? |
|
3.5.4.12 |
dCMP + H2O |
the enzyme is the major supplier of substrate for the thymidylate synthase important in DNA synthesis |
Tequatrovirus T4 |
dUMP + NH3 |
- |
? |
|
Subunits
EC Number |
Subunits |
Comment |
Organism |
---|
3.5.4.12 |
dimer |
the mutant R115E is dimeric in solution, while hexameric in crystals, quarternary structure analysis |
Tequatrovirus T4 |
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
3.5.4.12 |
2-deoxycytidylate deaminase |
- |
Tequatrovirus T4 |
3.5.4.12 |
DCD |
- |
Tequatrovirus T4 |