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

BRENDA support

Literature summary for 6.3.5.5 extracted from

  • Fan, Y.; Lund, L.; Yang, L.; Raushel, F.M.; Gao, Y.Q.
    Mechanism for the transport of ammonia within carbamoyl phosphate synthetase determined by molecular dynamics simulations (2008), Biochemistry, 47, 2935-2944.
    View publication on PubMed

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+
-
Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
40000
-
x * 40000 + x * 118000 Escherichia coli
118000
-
x * 40000 + x * 118000 Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + L-glutamine + HCO3- + H2O Escherichia coli CPS1 plays a critical role in the biosynthesis of pyrimidine nucleotides and the detoxification of ammonia ADP + phosphate + L-glutamate + carbamoyl phosphate
-
?
additional information Escherichia coli CPS uses the hydrolysis of glutamine as a localized source of ammonia for biosynthetic transformations ?
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Reaction

Reaction Comment Organism Reaction ID
2 ATP + L-glutamine + hydrogencarbonate + H2O = 2 ADP + phosphate + L-glutamate + carbamoyl phosphate reaction mechanism, the ammonium is channeled as ammonia through a channel formed by the small subunit by forming and breaking hydrogen bonds to Gly292, Ser35, Pro358, Gly293, and Thr37 in a stepwise fashion as it travels through the hydrophilic passage toward the subunit interface Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-glutamine + HCO3- + H2O CPS1 plays a critical role in the biosynthesis of pyrimidine nucleotides and the detoxification of ammonia Escherichia coli ADP + phosphate + L-glutamate + carbamoyl phosphate
-
?
ATP + L-glutamine + HCO3- + H2O the enzyme from Escherichia coli catalyzes the synthesis of carbamoyl phosphate from bicarbonate, glutamine, and two molecules of ATP via a chemical mechanism that involves four separate reactions and three unstable intermediates, e.g. carboxyphosphate and carbamate Escherichia coli ADP + phosphate + L-glutamate + carbamoyl phosphate
-
r
additional information CPS uses the hydrolysis of glutamine as a localized source of ammonia for biosynthetic transformations Escherichia coli ?
-
?
additional information the smaller subunit contains the binding site for the hydrolysis of glutamine, whereas the large subunit catalyzes the formation of carbamoyl phosphate. Molecular dynamics simulations and free-energy profile for the transfer of ammonia and ammonium through a tunnel in the small subunit of CPS, by use of the enzyme's crystal structure, resulting in five successful trajectories for ammonia transfer, while ammonium is immobilized in a water pocket inside the small subunit of the heterodimeric protein, the carbamate tunnel connects the two active sites within the large subunit to one another and guides the unstable carbamate intermediate to the site of phosphorylation, mechanism, overview Escherichia coli ?
-
?

Subunits

Subunits Comment Organism
? x * 40000 + x * 118000 Escherichia coli
More the smaller subunit contains the binding site for the hydrolysis of glutamine, whereas the large subunit catalyzes the formation of carbamoyl phosphate. The enzyme posssesses three distinct active sites and an ammonia tunnel, that starts at the active site in the small subunit and leads to the active site in the N-terminal domain of the large subunit Escherichia coli

Synonyms

Synonyms Comment Organism
carbamoyl phosphate synthetase
-
Escherichia coli
carbamoyl phosphate synthetase 1
-
Escherichia coli
CPS
-
Escherichia coli
CPS1
-
Escherichia coli
More carbamoyl phosphate synthetase is a member of the amidotransferase family of enzymes Escherichia coli

Cofactor

Cofactor Comment Organism Structure
ATP
-
Escherichia coli