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Literature summary extracted from

  • Rishavy, M.A.; Cleland, W.W.; Lusty, C.J.
    15N isotope effects in glutamine hydrolysis catalyzed by carbamyl phosphate synthetase: evidence for a tetrahedral intermediate in the mechanism (2000), Biochemistry, 39, 7309-7315.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
6.3.5.5 E841K comparison of 15N-isotope effects in mutant and wild-type enzyme on the hydrolysis of glutamine, the rate of glutamine hydrolysis in the mutant is not affected by MgATP2 and HCO3-, with the wild-type enzyme in the absence of MgATP2 and HCO3- the isotope effect id reduced Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
6.3.5.5 0.15
-
L-glutamine pH 7.6, 37°C, L-glutamine hydrolysis 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
-
2 ADP + phosphate + L-Glu + carbamoyl phosphate
-
ir

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 An ordered uni bi mechanism for glutamine hydrolysis that is consistent with the isotope effects and with the catalytic properties of the enzyme is proposed Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.3.5.5 2 ATP + L-Gln + HCO3-
-
Escherichia coli 2 ADP + phosphate + L-Glu + carbamoyl phosphate
-
ir

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
6.3.5.5 4.2
-
wild-type enzyme Escherichia coli
6.3.5.5 6.6
-
mutant enzyme E841K Escherichia coli
6.3.5.5 9.3
-
wild-type enzyme Escherichia coli