Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Saeed-Kothe, A.; Powers-Lee, S.G.
    Gain of glutaminase function in mutants of the ammonia-specific frog carbamoyl phosphate synthetase (2003), J. Biol. Chem., 278, 26722-26726.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
6.3.4.16 expression in Saccharomyces pombe Lithobates catesbeianus

Protein Variants

EC Number Protein Variants Comment Organism
6.3.4.16 E261Q no synthesis of carbonyl phosphate in presence of L-glutamine Lithobates catesbeianus
6.3.4.16 K258L synthesis of carbonyl phosphate in presence of L-glutamine Lithobates catesbeianus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
6.3.4.16 0.27
-
ATP wild-type enzyme, comparison to native and mutant enzyme Lithobates catesbeianus
6.3.4.16 0.39
-
ammonia wild-type enzyme, comparison to native and mutant enzyme Lithobates catesbeianus
6.3.5.5 0.05
-
ATP glutamine-dependent ADP formation Escherichia coli
6.3.5.5 0.06
-
ATP ammonia-dependent ADP formation Escherichia coli
6.3.5.5 0.17
-
L-glutamine
-
Escherichia coli
6.3.5.5 111
-
ammonia
-
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- Homo sapiens
-
2 ADP + phosphate + carbamoyl phosphate
-
?
6.3.4.16 2 ATP + NH4+ + HCO3- Rattus norvegicus
-
2 ADP + phosphate + carbamoyl phosphate
-
?
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 product carbamoyl phosphate is utilized for the arginine biosynthesis 2 ADP + phosphate + L-Glu + carbamoyl phosphate
-
?

Organism

EC Number Organism UniProt Comment Textmining
6.3.4.16 Homo sapiens
-
-
-
6.3.4.16 Lithobates catesbeianus
-
-
-
6.3.4.16 Rattus norvegicus
-
-
-
6.3.5.5 Escherichia coli
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
6.3.4.16
-
Lithobates catesbeianus

Reaction

EC Number Reaction Comment Organism Reaction ID
6.3.4.16 2 ATP + NH3 + hydrogencarbonate = 2 ADP + phosphate + carbamoyl phosphate depending on their physiological role, carbonyl phosphate synthetases use either glutamine or free ammonia as the nitrogen donor for carbamoyl phosphate synthesis, all enzymes contain the structurally equivalent of a triad-type glutamine amidotransferase, GAT, domain Lithobates catesbeianus
6.3.4.16 2 ATP + NH3 + hydrogencarbonate = 2 ADP + phosphate + carbamoyl phosphate depending on their physiological role, carbonyl phosphate synthetases uses either glutamine or free ammonia as the nitrogen donor for carbamoyl phosphate synthesis, all enzymes contain the structurell equivalent of a triad-type glutamine amidotransferase, GAT, domain Homo sapiens
6.3.4.16 2 ATP + NH3 + hydrogencarbonate = 2 ADP + phosphate + carbamoyl phosphate depending on their physiological role, carbonyl phosphate synthetasese uses either glutamine or free ammonia as the nitrogen donor for carbamoyl phosphate synthesis, all enzymes contain the structurell equivalent of a triad-type glutamine amidotransferase, GAT, domain Rattus norvegicus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.3.4.16 2 ATP + NH4+ + HCO3-
-
Homo sapiens 2 ADP + phosphate + carbamoyl phosphate
-
?
6.3.4.16 2 ATP + NH4+ + HCO3-
-
Rattus norvegicus 2 ADP + phosphate + carbamoyl phosphate
-
?
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 2 ADP + phosphate + L-Glu + carbamoyl phosphate
-
?
6.3.5.5 2 ATP + L-Gln + HCO3- the product carbamoyl phosphate is utilized for the arginine biosynthesis Escherichia coli 2 ADP + phosphate + L-Glu + carbamoyl phosphate
-
?
6.3.5.5 2 ATP + NH4+ + HCO3-
-
Escherichia coli 2 ADP + phosphate + carbamoyl phosphate
-
?

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
6.3.4.16 1.8
-
ammonia wild-type enzyme, comparison to native and mutant enzyme Lithobates catesbeianus
6.3.4.16 2.4
-
ATP wild-type enzyme, comparison to native and mutant enzyme Lithobates catesbeianus
6.3.5.5 2.2
-
ATP ammonia-dependent ADP formation Escherichia coli
6.3.5.5 5.1
-
ammonia
-
Escherichia coli
6.3.5.5 6.8
-
ATP glutamine-dependent ADP formation Escherichia coli
6.3.5.5 9.4
-
L-glutamine
-
Escherichia coli