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Literature summary for 6.3.5.5 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
Search for more literature for 6.3.5.5

Protein Variants

Protein Variants Comment Organism
G359F Km values of L-glutamine are increased Escherichia coli
G359L Km values of L-glutamine are increased Escherichia coli
G359S Km values of L-glutamine are increased Escherichia coli
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
S35F kinetic properties are similar to the wild-type enzyme, only KM-value of L-glutamine is 5fold increased Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
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)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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

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 mechanism Escherichia coli
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 ATP + gamma-glutamyl hydrazide + HCO3-
-
 Escherichia coli ?
-
 ?
2 ATP + gamma-glutamyl hydroxamate + HCO3-
-
 Escherichia coli ?
-
 ?
2 ATP + hydrazine + HCO3-
-
 Escherichia coli 2 ADP + phosphate + N-amino carbamoyl phosphate
-
 ?
2 ATP + hydroxylamine + HCO3-
-
 Escherichia coli 2 ADP + phosphate + N-hydroxy carbamoyl phosphate
-
 ?
2 ATP + L-Gln + HCO3-
-
 Escherichia coli 2 ADP + phosphate + L-Glu + carbamoyl phosphate
-
 ?
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
-
 ?
2 ATP + NH4+ + HCO3-
-
 Escherichia coli 2 ADP + phosphate + carbamoyl phosphate
-
 ?

Subunits

Subunits Comment Organism
heterodimer
-
 Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
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