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Literature summary for 3.5.4.12 extracted from

  • Mollgaard, H.; Neuhard, J.
    Deoxycytidylate deaminase from Bacillus subtilis. Purification, characterization, and physiological function (1978), J. Biol. Chem., 253, 3536-3542.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
2-mercaptoethanol enzyme requires dCTP, Zn2+, and 2-mercaptoethanol Bacillus subtilis
CTP no activation Bacillus subtilis
dCDP 100% activation Bacillus subtilis
dCTP dCTP not required and not activared by dCTP Bacillusphage phiE
dCTP dCTP not required and not activared by dCTP bacteriophage SP8
dCTP required, enzyme requires dCTP, Zn2+, and 2-mercaptoethanol Bacillus subtilis
dTTP no activation Bacillus subtilis
dUTP 89% activation Bacillus subtilis
additional information no activation by ATP, UTP, CTP and dTTP Bacillus subtilis

General Stability

General Stability Organism
2-mercaptoethanol stabilizes Bacillus subtilis
thiols stabilize Bacillus subtilis
thiols, such as 2-mercaptoethanol or dithiothreitol, stabilize, in the absence of thiols the enzyme is highly unstable Bacillus subtilis
Zn2+ or dCTP stabilize, protect against inactivation Bacillus subtilis

Inhibitors

Inhibitors Comment Organism Structure
dTTP no inhibition by dTTP bacteriophage SP8
EDTA completely Bacillus subtilis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information
-
Bacillus subtilis
0.14
-
dCMP
-
Bacillus subtilis

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ no activation Bacillus subtilis
Co2+ metal ion required, highest activity with Zn2+, about 20% activity with Co2+, Mn2+, and Ni2+ Bacillus subtilis
metal ion required, in the absence of metal ions: 40% activity, Zn2+ highest activity, around 20% activity with Co2+, Mn2+, and Ni2+, no activity in the presence of Mg2+, Ca2+ and Fe2+ Bacillus subtilis
Mg2+ no activation Bacillus subtilis
Mg2+ enzyme requires dCTP, Zn2+, and 2-mercaptoethanol, Mg2+ cannot substitute for Zn2+ Bacillus subtilis
Mn2+ metal ion required, highest activity with Zn2+, about 20% activity with Co2+, Mn2+, and Ni2+ Bacillus subtilis
additional information metal ions not required Bacillusphage phiE
additional information metal ions not required bacteriophage SP8
additional information metal ion required, in the absence of metal ions: 40% activity, Zn2+ highest activity, around 20% activity with Co2+, Mn2+, and Ni2+, no activity in the presence of Mg2+, Ca2+ and Fe2+ Bacillus subtilis
Ni2+ metal ion required, highest activity with Zn2+, about 20% activity with Co2+, Mn2+, and Ni2+ Bacillus subtilis
Zn2+ required, enzyme requires dCTP, Zn2+, and 2-mercaptoethanol, Mg2+ cannot substitute for Zn2+ Bacillus subtilis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
170000
-
gel filtration and sucrose density gradient centrifugation Bacillus subtilis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
dCMP + H2O Bacillus subtilis importance in the generation of dUMP, precursor for synthesis of thymidine nucleotides dUMP + NH3
-
?
dCMP + H2O Bacillus subtilis ED40 importance in the generation of dUMP, precursor for synthesis of thymidine nucleotides dUMP + NH3
-
?

Organism

Organism UniProt Comment Textmining
Bacillus subtilis
-
-
-
Bacillus subtilis ED40
-
-
-
Bacillusphage phiE
-
host Bacillus subtilis
-
bacteriophage SP8
-
host Bacillus subtilis
-
no activity in Escherichia coli
-
wild type Escherichia coli contains no dCMP deaminase
-
no activity in Salmonella typhimurium
-
do not contain dCMP deaminase
-

Purification (Commentary)

Purification (Comment) Organism
partial Bacillus subtilis

Reaction

Reaction Comment Organism Reaction ID
dCMP + H2O = dUMP + NH3 regulation, allosteric end-product regulation Bacillus subtilis
dCMP + H2O = dUMP + NH3 highly regulated allosteric enzyme Bacillus subtilis

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
6.36
-
-
Bacillus subtilis

Storage Stability

Storage Stability Organism
-70°C, pH 7.8, 2 mM 2-mercaptoethanol Bacillus subtilis
0°C, 2-mercaptoethanol, stable for more than 6 h Bacillus subtilis
0°C, half-life: 30 min Bacillus subtilis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
CMP + H2O slight activity, about 5% compared with dCMP Bacillus subtilis UMP + NH3
-
?
CMP + H2O slight activity, about 5% compared with dCMP Bacillus subtilis ED40 UMP + NH3
-
?
dCMP + H2O
-
Bacillus subtilis dUMP + NH3
-
?
dCMP + H2O
-
Bacillusphage phiE dUMP + NH3
-
?
dCMP + H2O
-
bacteriophage SP8 dUMP + NH3
-
?
dCMP + H2O importance in the generation of dUMP, precursor for synthesis of thymidine nucleotides Bacillus subtilis dUMP + NH3
-
?
dCMP + H2O
-
Bacillus subtilis ED40 dUMP + NH3
-
?
dCMP + H2O importance in the generation of dUMP, precursor for synthesis of thymidine nucleotides Bacillus subtilis ED40 dUMP + NH3
-
?
additional information substrate specificity Bacillus subtilis ?
-
?
additional information no activity with dCDP, dCTP, CDP, CTP Bacillus subtilis ?
-
?
additional information substrate specificity Bacillus subtilis ED40 ?
-
?
additional information no activity with dCDP, dCTP, CDP, CTP Bacillus subtilis ED40 ?
-
?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Bacillus subtilis

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
-
-
half-life: 30 min, Zn2+, thiols, 2-mercaptoethanol, and dCTP protect against inactivation Bacillus subtilis
50
-
thiol, 2-mercaptoethanol, dCTP and Zn2+ protect the enzyme against heat inactivation at 50°C Bacillus subtilis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.8
-
pH optimum around Bacillus subtilis

pH Range

pH Minimum pH Maximum Comment Organism
7 8.5 50% maximal activity at pH 7.0 and 8.5 Bacillus subtilis