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Literature summary for 6.3.4.2 extracted from

  • Willemös, M.
    Competition between ammonia derived from internal glutamine hydrolysis and hydroxylamine present in the solution for incorporation into UTP as catalysed by Lactococcus lactis CTP synthase (2004), Arch. Biochem. Biophys., 424, 105-111.
    View publication on PubMed
Search for more literature for 6.3.4.2

Activating Compound

Activating Compound Comment Organism Structure
GTP stimulates reaction with ATP, UTP and Gln Lactococcus lactis

Inhibitors

Inhibitors Comment Organism Structure
DL-DELTA1-pyrroline 5-carboxylate 0.125 mM, complete inhibition of ammonium chloride-dependent CTP synthesis Lactococcus lactis
Gln inhibition of hydroxylamine-dependent N4-OH CTP synthesis in presence of GTP Lactococcus lactis
GTP inhibition of N4-OH-CTP synthesis Lactococcus lactis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.259
-
 Gln 30°C, pH 8.0 Lactococcus lactis

Organism

Organism UniProt Comment Textmining
Lactococcus lactis
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + UTP + Gln
-
 Lactococcus lactis ADP + phosphate + CTP + Glu
-
 ?
ATP + UTP + hydroxylamine
-
 Lactococcus lactis ADP + phosphate + N4-OH-CTP
-
 ?
ATP + UTP + NH4+
-
 Lactococcus lactis ADP + phosphate + CTP
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.49
-
 Gln 30°C, pH 8.0 Lactococcus lactis

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.182
-
 Gln 30°C, pH 8.0, inhibition of hydroxylamine-dependent N4-OH CTP synthesis in presence of GTP Lactococcus lactis
0.366
-
 GTP 30°C, pH 8.0, inhibition of N4-OH-CTP synthesis Lactococcus lactis