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Literature summary extracted from

  • Mori, M.; Tatibana, M.
    Glutaminase activity of glutamine-dependent carbamoylphosphate synthase from rat ascites hepatoma. Regulation by adenosine triphosphate-magnesium and magnesium ion (1977), Biochim. Biophys. Acta, 483, 90-99.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
6.3.5.5 Ala inhibits glutamine hydrolysis and Gln-dependent carbamoyl phosphate synthesis Rattus norvegicus
6.3.5.5 Gly 10 mM, inhibition of glutaminase activity Rattus norvegicus
6.3.5.5 L-Glu inhibits glutaminase activity moderately Rattus norvegicus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
6.3.5.5 Mg2+ MgATP2- or Mg2+ enhances glutaminase activity Rattus norvegicus

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- Rattus norvegicus catalyzes the first step of de novo pyrimidine biosynthesis ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
6.3.5.5 Rattus norvegicus
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
6.3.5.5 hepatoma ascites cell AH13 Rattus norvegicus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.3.5.5 2 ATP + L-Gln + HCO3-
-
 Rattus norvegicus 2 ADP + phosphate + L-Glu + carbamoyl phosphate
-
 ?
6.3.5.5 ATP + L-Gln + HCO3- catalyzes the first step of de novo pyrimidine biosynthesis Rattus norvegicus ?
-
 ?
6.3.5.5 additional information hydrolysis of L-Gln in absence of the other substrates, at 5.9% the rate of glutamine hydrolysis in the complete system Rattus norvegicus ?
-
 ?