Data extracted from this reference:
Cloned(Commentary)
3.5.4.5
enzyme expression in Escherichia coli strain BL21
Mus musculus
Crystallization (Commentary)
3.5.4.5
in complex with tetrahydrouridine, 3-deazauridine, or cytidine. Two alternate conformations of R68 influence zinc-product interaction; purified recombinant CDA complexed with either tetrahydrouridine, 3-deazauridine, or cytidine, hanging drop vapor diffusion technique, 25°C, protein solution, containing 10-15 mg/ml protein in 20 mM Tris-HCl, pH 7.5, 1 mM DTT, and 5 mM ligand, is mixed with crystallization solution containing 2.0 M ammonium sulfate and 0.1 M Tris-HCl, pH 8.5, crystals appear after a few hours or several days, respectively, X-ray diffraction structure determination and analysis at 1.48-2.36 A resolutions, molecular replacement
Mus musculus
Inhibitors
3.5.4.5
3-deazauridine
Mus musculus
3.5.4.5
tetrahydrouridine
Mus musculus
Metals/Ions
3.5.4.5
Zn2+
catalytic ion, coordinated by C65, C99, and C102; dependent on
Mus musculus
Natural Substrates/ Products (Substrates)
3.5.4.5
2'-deoxycytidine + H2O
Mus musculus
2'-deoxyuridine + NH3
?
3.5.4.5
cytidine + H2O
Mus musculus
uridine + NH3
?
Organism
3.5.4.5
Mus musculus
P56389
Purification (Commentary)
3.5.4.5
recombinant enzyme from Escherichia coli strain BL21 by two steps of anion exchange chromatography, and gel filtration
Mus musculus
Substrates and Products (Substrate)
3.5.4.5
2'-deoxycytidine + H2O
667736
Mus musculus
2'-deoxyuridine + NH3
?
3.5.4.5
cytidine + H2O
667736
Mus musculus
uridine + NH3
?
3.5.4.5
cytidine + H2O
cytidine is distinguished from uridine by its 4-NH2 group that acts as a hydrogen bond donor, the charge-neutralizing Arg68 of CDA exhibits two alternate conformations I and II, binding structure, overview
667736
Mus musculus
uridine + NH3
?
3.5.4.5
additional information
active site and substrate binding structure, overview
667736
Mus musculus
?
Subunits
3.5.4.5
tetramer
homotetramer
Mus musculus
Synonyms
Cloned(Commentary) (protein specific)
3.5.4.5
enzyme expression in Escherichia coli strain BL21
Mus musculus
Crystallization (Commentary) (protein specific)
3.5.4.5
in complex with tetrahydrouridine, 3-deazauridine, or cytidine. Two alternate conformations of R68 influence zinc-product interaction; purified recombinant CDA complexed with either tetrahydrouridine, 3-deazauridine, or cytidine, hanging drop vapor diffusion technique, 25°C, protein solution, containing 10-15 mg/ml protein in 20 mM Tris-HCl, pH 7.5, 1 mM DTT, and 5 mM ligand, is mixed with crystallization solution containing 2.0 M ammonium sulfate and 0.1 M Tris-HCl, pH 8.5, crystals appear after a few hours or several days, respectively, X-ray diffraction structure determination and analysis at 1.48-2.36 A resolutions, molecular replacement
Mus musculus
Inhibitors (protein specific)
3.5.4.5
3-deazauridine
Mus musculus
3.5.4.5
tetrahydrouridine
Mus musculus
Metals/Ions (protein specific)
3.5.4.5
Zn2+
catalytic ion, coordinated by C65, C99, and C102; dependent on
Mus musculus
Natural Substrates/ Products (Substrates) (protein specific)
3.5.4.5
2'-deoxycytidine + H2O
Mus musculus
2'-deoxyuridine + NH3
?
3.5.4.5
cytidine + H2O
Mus musculus
uridine + NH3
?
Purification (Commentary) (protein specific)
3.5.4.5
recombinant enzyme from Escherichia coli strain BL21 by two steps of anion exchange chromatography, and gel filtration
Mus musculus
Substrates and Products (Substrate) (protein specific)
3.5.4.5
2'-deoxycytidine + H2O
667736
Mus musculus
2'-deoxyuridine + NH3
?
3.5.4.5
cytidine + H2O
667736
Mus musculus
uridine + NH3
?
3.5.4.5
cytidine + H2O
cytidine is distinguished from uridine by its 4-NH2 group that acts as a hydrogen bond donor, the charge-neutralizing Arg68 of CDA exhibits two alternate conformations I and II, binding structure, overview
667736
Mus musculus
uridine + NH3
?
3.5.4.5
additional information
active site and substrate binding structure, overview
667736
Mus musculus
?
Subunits (protein specific)
3.5.4.5
tetramer
homotetramer
Mus musculus