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Literature summary for 3.5.4.1 extracted from

  • Porter, D.J.T.
    Escherichia coli cytosine deaminase: the kinetics and thermodynamics for binding of cytosine to the apoenzyme and the Zn2+ holoenzyme are similar (2000), Biochim. Biophys. Acta, 1476, 239-252.
    View publication on PubMed
Search for more literature for 3.5.4.1

Cloned(Commentary)

Cloned (Comment) Organism
-
 Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
o-phenanthroline removes Fe2+ from the Fe2+CDase to give the apoenzyme, cause of loss in activity, reversible by Fe2+ addition, poor effect on Zn2+CDase Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information pre-steady-state and steady-state kinetics and thermodynamics of cytosine substrate binding to apoenzyme and Zn2+-holoenzyme Escherichia coli
0.1
-
 2-thiocytosine pH 7.5, 25°C, CDase Escherichia coli
0.109
-
 2-thiocytosine pH 7.5, 25°C, Zn2+CDase Escherichia coli
0.12
-
 5-Azacytosine pH 7.5, 25°C, CDase Escherichia coli
0.2
-
 cytosine pH 7.5, 25°C, CDase Escherichia coli
0.2
-
 cytosine pH 7.5, 25°C, Zn2+CDase Escherichia coli
0.36
-
 5-Azacytosine pH 7.5, 25°C, Zn2+CDase Escherichia coli
1.02
-
 6-azacytosine pH 7.5, 25°C, Zn2+CDase Escherichia coli
1.6
-
 6-azacytosine pH 7.5, 25°C, CDase Escherichia coli
1.7
-
 5-fluorocytosine pH 7.5, 25°C, CDase Escherichia coli
11.2
-
 5-fluorocytosine pH 7.5, 25°C, Zn2+CDase Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ bound to the enzyme, very rapid complex formation Escherichia coli
Zn2+ bound to the enzyme, below 0.2 mol per mol of subunit, reconstitution of apoenzyme Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
 enzyme is encoded in codBA operon
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme as a mixture of Zn2+ and Fe2+ enzyme forms Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-thiocytosine + H2O
-
 Escherichia coli 2-thiouracil + NH3
-
 ?
5-azacytosine + H2O
-
 Escherichia coli 5-azauracil + NH3
-
 ?
5-fluorocytosine + H2O low activity Escherichia coli 5-fluorouracil + NH3
-
 ?
6-azacytosine + H2O
-
 Escherichia coli 6-azauracil + NH3
-
 ?
cytosine + H2O best substrate Escherichia coli uracil + NH3
-
 ?
additional information creatinine is a poor substrate for Zn2+CDase and apoCDase Escherichia coli ?
-
 ?

Synonyms

Synonyms Comment Organism
CDase
-
 Escherichia coli
Zn2+CDase
-
 Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
 assay at Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.65
-
 5-Azacytosine pH 7.5, 25°C, Zn2+CDase Escherichia coli
2.27
-
 2-thiocytosine pH 7.5, 25°C, Zn2+CDase Escherichia coli
2.68
-
 5-Azacytosine pH 7.5, 25°C, CDase Escherichia coli
5.4
-
 6-azacytosine pH 7.5, 25°C, Zn2+CDase Escherichia coli
5.5
-
 5-fluorocytosine pH 7.5, 25°C, Zn2+CDase Escherichia coli
16
-
 5-fluorocytosine pH 7.5, 25°C, CDase Escherichia coli
22.3
-
 2-thiocytosine pH 7.5, 25°C, CDase Escherichia coli
26.4
-
 cytosine pH 7.5, 25°C, Zn2+CDase Escherichia coli
185
-
 cytosine pH 7.5, 25°C, CDase Escherichia coli
186
-
 6-azacytosine pH 7.5, 25°C, CDase Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 assay at Escherichia coli