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Literature summary extracted from

  • Aoki, T.; Oya, H.
    Inactivation of Crithidia fasciculata carbamoyl phosphate synthetase II by the antitumor drug acivicin (1987), Mol. Biochem. Parasitol., 23, 173-181.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
6.3.5.5 acivicin selective time-dependent inhibition of L-Gln-dependent activity, L-Gln protects the enzyme from inactivation. Stimulation of NH4+-dependent activity Crithidia fasciculata

Inhibitors

EC Number Inhibitors Comment Organism Structure
6.3.5.5 acivicin selective time-dependent inhibition of L-Gln-dependent activity, L-Gln protects the enzyme from inactivation. Stimulation of NH4+-dependent activity Crithidia fasciculata

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
6.3.5.5 ATP + L-Gln + HCO3- Crithidia fasciculata catalyzes the first step of de novo pyrimidine biosynthesis ?
-
?

Organism

EC Number Organism UniProt Comment Textmining
6.3.5.5 Crithidia fasciculata
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.3.5.5 2 ATP + L-Gln + HCO3-
-
Crithidia fasciculata 2 ADP + phosphate + L-Glu + carbamoyl phosphate
-
?
6.3.5.5 ATP + L-Gln + HCO3- catalyzes the first step of de novo pyrimidine biosynthesis Crithidia fasciculata ?
-
?