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Literature summary for 6.3.4.2 extracted from

  • Robertson, J.G.; Villafranca, J.J.
    Characterization of metal ion activation and inhibition of CTP synthetase (1993), Biochemistry, 32, 3769-3777.
    View publication on PubMed
Search for more literature for 6.3.4.2

Inhibitors

Inhibitors Comment Organism Structure
Co2+ above 2 mM Escherichia coli
Cu2+ inhibition is not reversed by EDTA, in presence of dithiothreitol inhibition at concentrations below 0.2 mM Escherichia coli
Mn2+ above 2 mM Escherichia coli
Ni2+ in presence of dithiothreitol inhibition at concentrations below 0.2 mM Escherichia coli
Zn2+ inhibition is reversed by EDTA, in presence of dithiothreitol inhibition at concentrations below 0.2 mM Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+ stimulates at a lower level than Mg2+ Escherichia coli
Mg2+ the enzyme requires more Mg2+ for full catalytic activity than required simply to complex the nucleotide substrate. Half-saturation value for Mg2+ is 2.6 mM for the reaction with NH4+ and 2.4 mM for the glutamine-dependent reaction Escherichia coli
Mn2+ stimulates at a lower level than Mg2+ Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + UTP + NH4+
-
 Escherichia coli ADP + phosphate + CTP
-
 ?

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
 glutamine-dependent reaction activated by Co2+ Escherichia coli
8.7
-
 reaction with NH4+, glutamine-dependent reaction activated by Mg2+ or Mn2+ Escherichia coli