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Literature summary extracted from

  • Huang, X.; Raushel, F.M.
    Restricted passage of reaction intermediates through the ammonia tunnel of carbamoyl phosphate synthetase (2000), J. Biol. Chem., 275, 26233-26240.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
6.3.5.5 G359F Km values of L-glutamine are increased Escherichia coli
6.3.5.5 G359L Km values of L-glutamine are increased Escherichia coli
6.3.5.5 G359S Km values of L-glutamine are increased Escherichia coli
6.3.5.5 additional information A series of mutants created within the ammonia tunnel are prepared by placement of a constriction via site-directed mutagenesis. The degree of constriction within the ammonia tunnel of these enzymes is found to correlate to the extent of the uncoupling of the partial reactions, the diminution of carbamoyl phosphate formation, and the percentage of the internally derived ammonia that is channelled through the ammonia tunnel Escherichia coli
6.3.5.5 S35F kinetic properties are similar to the wild-type enzyme, only KM-value of L-glutamine is 5fold increased 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 Km values for the formation of ADP, glutamate and carbonyl phosphate of the wild-type and mutant enzymes, Km values for the hydrolysis of gamma-glutamyl hydroxamate, gamma-glutamyl hydrazide, gamma-glutamyl hydroxamate and hydroxylamine of the wild-type and mutant enzymes Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
6.3.5.5 2 ATP + L-Gln + HCO3- Escherichia coli the enzyme catalyses the entry and rate-limiting step of the urea cycle 2 ADP + phosphate + L-Glu + carbamoyl phosphate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
6.3.5.5 Escherichia coli
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
6.3.5.5 2 ATP + L-glutamine + hydrogencarbonate + H2O = 2 ADP + phosphate + L-glutamate + carbamoyl phosphate mechanism Escherichia coli
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.3.5.5 2 ATP + gamma-glutamyl hydrazide + HCO3-
-
 Escherichia coli ?
-
 ?
6.3.5.5 2 ATP + gamma-glutamyl hydroxamate + HCO3-
-
 Escherichia coli ?
-
 ?
6.3.5.5 2 ATP + hydrazine + HCO3-
-
 Escherichia coli 2 ADP + phosphate + N-amino carbamoyl phosphate
-
 ?
6.3.5.5 2 ATP + hydroxylamine + HCO3-
-
 Escherichia coli 2 ADP + phosphate + N-hydroxy 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 enzyme catalyses the entry and rate-limiting step of the urea cycle Escherichia coli 2 ADP + phosphate + L-Glu + carbamoyl phosphate
-
 ?
6.3.5.5 2 ATP + NH4+ + HCO3-
-
 Escherichia coli 2 ADP + phosphate + carbamoyl phosphate
-
 ?

Subunits

EC Number Subunits Comment Organism
6.3.5.5 heterodimer
-
 Escherichia coli

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 kcat values for the formation of ADP, glutamate and carbonyl phosphate of the wild-type and mutant enzymes, kcat values for the hydrolysis of gamma-glutamyl hydroxamate, gamma-glutamyl hydrazide, gamma-glutamyl hydroxamate and hydroxylamine of the wild-type and mutant enzymes Escherichia coli