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Literature summary extracted from

  • Willemoes, M.; Sigurskjold, B.W.
    Steady-state kinetics of the glutaminase reaction of CTP synthase from Lactococcus lactis. The role of the allosteric activator GTP incoupling between glutamine hydrolysis and CTP synthesis (2002), Eur. J. Biochem., 269, 4772-4779.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
6.3.4.2 GTP the binding of GTP to the allosteric site promotes coordination of the phosphorylation of UTP and hydrolysis of glutamine for optimal efficiency in CTP synthesis rather than just acting to increase the rate of glutamine hydrolysis itself Lactococcus lactis

Inhibitors

EC Number Inhibitors Comment Organism Structure
6.3.4.2 adenosine 5'-[beta,gamma-imido]triphosphate poor inhibitor compared to ATPgammaS Lactococcus lactis
6.3.4.2 ATPgammaS
-
 Lactococcus lactis

Organism

EC Number Organism UniProt Comment Textmining
6.3.4.2 Lactococcus lactis
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.3.4.2 ATP + UTP + glutamine
-
 Lactococcus lactis ADP + phosphate + CTP + Glu
-
 ?
6.3.4.2 ATP + UTP + NH4+
-
 Lactococcus lactis ADP + phosphate + CTP
-
 ?

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
6.3.4.2 additional information
-
 additional information
-
 Lactococcus lactis