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Literature summary for 6.3.5.5 extracted from

  • Avid-Majd, F.; Stapleton, M.A.; Harmon, M.F.; Hanks, B.A.; Mullins, L.S.; Raushel, F.M.
    Comparison of the functional differences for the homologous residues within the carboxy phosphate and carbamate domains of carbamoyl phosphate synthetase (1996), Biochemistry, 35, 14362-14369.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
D753X residues within the carbamate domain of the large subunit of CPS are selected as targets for mutagenesis. Mutant enzymes E761A, E841Q, N843D, R845Q have diminished ability to synthesize carbamoyl phosphate. Mutant enzymes R715A, Q829A, and R675A show elevated Michaelis constants for MgATP2- in the partial back reaction. The mutant enzymes E761A, N827A, E841Q, N843D, and R845Q show significant increases in the Michaelis constant for either bicarbonate or carbamoyl phosphate. No significant alterations are noted upon mutation of either R571 or D753 Escherichia coli
E761A residues within the carbamate domain of the large subunit of CPS are selected as targets for mutagenesis. Mutant enzymes E761A, E841Q, N843D, R845Q have diminished ability to synthesize carbamoyl phosphate. Mutant enzymes R715A, Q829A, and R675A show elevated Michaelis constants for MgATP2- in the partial back reaction. The mutant enzymes E761A, N827A, E841Q, N843D, and R845Q show significant increases in the Michaelis constant for either bicarbonate or carbamoyl phosphate. No significant alterations are noted upon mutation of either R571 or D753 Escherichia coli
E841Q residues within the carbamate domain of the large subunit of CPS are selected as targets for mutagenesis. Mutant enzymes E761A, E841Q, N843D, R845Q have diminished ability to synthesize carbamoyl phosphate. Mutant enzymes R715A, Q829A, and R675A show elevated Michaelis constants for MgATP2- in the partial back reaction. The mutant enzymes E761A, N827A, E841Q, N843D, and R845Q show significant increases in the Michaelis constant for either bicarbonate or carbamoyl phosphate. No significant alterations are noted upon mutation of either R571 or D753 Escherichia coli
N827A residues within the carbamate domain of the large subunit of CPS are selected as targets for mutagenesis. Mutant enzymes E761A, E841Q, N843D, R845Q have diminished ability to synthesize carbamoyl phosphate. Mutant enzymes R715A, Q829A, and R675A show elevated Michaelis constants for MgATP2- in the partial back reaction. The mutant enzymes E761A, N827A, E841Q, N843D, and R845Q show significant increases in the Michaelis constant for either bicarbonate or carbamoyl phosphate. No significant alterations are noted upon mutation of either R571 or D753 Escherichia coli
N843Q residues within the carbamate domain of the large subunit of CPS are selected as targets for mutagenesis. Mutant enzymes E761A, E841Q, N843D, R845Q have diminished ability to synthesize carbamoyl phosphate. Mutant enzymes R715A, Q829A, and R675A show elevated Michaelis constants for MgATP2- in the partial back reaction. The mutant enzymes E761A, N827A, E841Q, N843D, and R845Q show significant increases in the Michaelis constant for either bicarbonate or carbamoyl phosphate. No significant alterations are noted upon mutation of either R571 or D753 Escherichia coli
Q829A residues within the carbamate domain of the large subunit of CPS are selected as targets for mutagenesis. Mutant enzymes E761A, E841Q, N843D, R845Q have diminished ability to synthesize carbamoyl phosphate. Mutant enzymes R715A, Q829A, and R675A show elevated Michaelis constants for MgATP2- in the partial back reaction. The mutant enzymes E761A, N827A, E841Q, N843D, and R845Q show significant increases in the Michaelis constant for either bicarbonate or carbamoyl phosphate. No significant alterations are noted upon mutation of either R571 or D753 Escherichia coli
R571X residues within the carbamate domain of the large subunit of CPS are selected as targets for mutagenesis. Mutant enzymes E761A, E841Q, N843D, R845Q have diminished ability to synthesize carbamoyl phosphate. Mutant enzymes R715A, Q829A, and R675A show elevated Michaelis constants for MgATP2- in the partial back reaction. The mutant enzymes E761A, N827A, E841Q, N843D, and R845Q show significant increases in the Michaelis constant for either bicarbonate or carbamoyl phosphate. No significant alterations are noted upon mutation of either R571 or D753 Escherichia coli
R675A residues within the carbamate domain of the large subunit of CPS are selected as targets for mutagenesis. Mutant enzymes E761A, E841Q, N843D, R845Q have diminished ability to synthesize carbamoyl phosphate. Mutant enzymes R715A, Q829A, and R675A show elevated Michaelis constants for MgATP2- in the partial back reaction. The mutant enzymes E761A, N827A, E841Q, N843D, and R845Q show significant increases in the Michaelis constant for either bicarbonate or carbamoyl phosphate. No significant alterations are noted upon mutation of either R571 or D753 Escherichia coli
R715A residues within the carbamate domain of the large subunit of CPS are selected as targets for mutagenesis. Mutant enzymes E761A, E841Q, N843D, R845Q have diminished ability to synthesize carbamoyl phosphate. Mutant enzymes R715A, Q829A, and R675A show elevated Michaelis constants for MgATP2- in the partial back reaction. The mutant enzymes E761A, N827A, E841Q, N843D, and R845Q show significant increases in the Michaelis constant for either bicarbonate or carbamoyl phosphate. No significant alterations are noted upon mutation of either R571 or D753 Escherichia coli
R845Q residues within the carbamate domain of the large subunit of CPS are selected as targets for mutagenesis. Mutant enzymes E761A, E841Q, N843D, R845Q have diminished ability to synthesize carbamoyl phosphate. Mutant enzymes R715A, Q829A, and R675A show elevated Michaelis constants for MgATP2- in the partial back reaction. The mutant enzymes E761A, N827A, E841Q, N843D, and R845Q show significant increases in the Michaelis constant for either bicarbonate or carbamoyl phosphate. No significant alterations are noted upon mutation of either R571 or D753 Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

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