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Literature summary for 6.3.5.5 extracted from

  • Saeed-Kothe, A.; Powers-Lee, S.G.
    Specificity determining residues in ammonia- and glutamine-dependent carbamoyl phosphate synthetases (2002), J. Biol. Chem., 277, 7231-7238.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
ammonia
-
Escherichia coli
L-ornithine
-
Escherichia coli

Protein Variants

Protein Variants Comment Organism
L270K ammonia-dependent carbamoyl phosphate synthesis activity is very similar to that of the wild-type enzyme, L-glutamine-dependent carbamoyl phosphate synthesis activity is 5fold decreased in comparison to the wild-type enzyme, the glutamine binding is almost entirely abolished Escherichia coli
additional information the mutants are constructed to mimic the potentially significant substitutions which is observed in the frog enzyme and to allow determination of the effects of these changes on the glutamine binding ability of enzyme Escherichia coli
Q273E ammonia-dependent carbamoyl phosphate synthesis activity is very similar to that of the wild-type enzyme, L-glutamine-dependent carbamoyl phosphate synthesis activity is equivalent to the wild-type enzyme, but the mutant is 10fold impaired in its L-glutamine binding ability in comparison to wild-type enzyme Escherichia coli
Q273E/L270K ammonia-dependent carbamoyl phosphate synthesis activity is very similar to that of the wild-type enzyme, L-glutamine-dependent carbamoyl phosphate synthesis activity is 25fold decreased in comparison to the wild-type enzyme, the glutamine binding is almost entirely abolished Escherichia coli
Q273E/N240S ammonia-dependent carbamoyl phosphate synthesis activity is very similar to that of the wild-type enzyme, L-glutamine-dependent carbamoyl phosphate synthesis activity is equivalent to the wild-type enzyme Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
UMP
-
Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information comparison of Km-values for wild-type and mutant enzymes in absence and presence of ornithine Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2 ATP + L-Gln + HCO3- Escherichia coli the enzyme catalyses the first step in the synthesis of arginine and pyrimidine 2 ADP + phosphate + L-Glu + carbamoyl phosphate
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
wild-type and mutant enzyme Escherichia coli

Reaction

Reaction Comment Organism Reaction ID
2 ATP + L-glutamine + hydrogencarbonate + H2O = 2 ADP + phosphate + L-glutamate + carbamoyl phosphate in glutamine utilizing enzymes, the hydrolysis of glutamine to yield ammonia is catalyzed at a triad-type glutamine amidotransferase domain Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 ATP + L-Gln + HCO3-
-
Escherichia coli 2 ADP + phosphate + L-Glu + carbamoyl phosphate
-
?
2 ATP + L-Gln + HCO3- the enzyme catalyses the first step in the synthesis of arginine and pyrimidine Escherichia coli 2 ADP + phosphate + L-Glu + carbamoyl phosphate
-
?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
-
additional information comparison of kcat-values for wild-type and mutant enzymes in absence and presence of ornithine Escherichia coli