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Literature summary 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

EC Number Activating Compound Comment Organism Structure
6.3.5.5 ammonia
-
 Escherichia coli
6.3.5.5 L-ornithine
-
 Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
6.3.5.5 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
6.3.5.5 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
6.3.5.5 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
6.3.5.5 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
6.3.5.5 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

EC Number Inhibitors Comment Organism Structure
6.3.5.5 UMP
-
 Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
6.3.5.5 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)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
6.3.4.16 2 ATP + NH4+ + HCO3- Lithobates catesbeianus
-
 2 ADP + phosphate + carbamoyl phosphate
-
 ?
6.3.5.5 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

EC Number Organism UniProt Comment Textmining
6.3.4.16 Lithobates catesbeianus
-
-
-
6.3.5.5 Escherichia coli
-
-
-

Purification (Commentary)

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

Reaction

EC Number Reaction Comment Organism Reaction ID
6.3.4.16 2 ATP + NH3 + hydrogencarbonate = 2 ADP + phosphate + carbamoyl phosphate non-glutamine-utilizing enzymes, lacking the catalytic cysteine residue, can generate carbamoyl phosphate only in presence of free ammonia Lithobates catesbeianus
a
6.3.5.5 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
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.3.4.16 2 ATP + NH4+ + HCO3-
-
 Lithobates catesbeianus 2 ADP + phosphate + carbamoyl phosphate
-
 ?
6.3.4.16 additional information this enzyme is unable to bind and utilize L-glutamine Lithobates catesbeianus ?
-
 ?
6.3.5.5 2 ATP + L-Gln + HCO3-
-
 Escherichia coli 2 ADP + phosphate + L-Glu + carbamoyl phosphate
-
 ?
6.3.5.5 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]

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