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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.
    View publication on PubMed

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
a

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