Crystallization (Comment) | Organism |
---|---|
- |
Escherichia coli |
Protein Variants | Comment | Organism |
---|---|---|
D207A | mutations of the residues E215A, N283A, E299Q, N301D, and R303Q result in proteins which are unable to synthesize carbamoyl phosphate at a significant rate. The binding of bicarbonate is most affected by the mutagenesis of residues E215A, E299Q, N301D, and R303Q. The Km for ATP is most affected in the mutant enzymes R129A, R169A, Q285A, and N301D. No significant changes in the catalytic constants are observed in the mutants R82A and D207A. All of the mutations, with the exception of the N301D mutant, primarily effect the enzyme by altering the step for the phosphorylation of bicarbonate. Mutation N301D also disrupts the catalytic step involved in the phosphorylation of carbamate | Escherichia coli |
E215A | mutations of the residues E215A, N283A, E299Q, N301D, and R303Q result in proteins which are unable to synthesize carbamoyl phosphate at a significant rate. The binding of bicarbonate is most affected by the mutagenesis of residues E215A, E299Q, N301D, and R303Q. The Km for ATP is most affected in the mutant enzymes R129A, R169A, Q285A, and N301D. No significant changes in the catalytic constants are observed in the mutants R82A and D207A. All of the mutations, with the exception of the N301D mutant, primarily effect the enzyme by altering the step for the phosphorylation of bicarbonate. Mutation N301D also disrupts the catalytic step involved in the phosphorylation of carbamate | Escherichia coli |
E299Q | mutations of the residues E215A, N283A, E299Q, N301D, and R303Q result in proteins which are unable to synthesize carbamoyl phosphate at a significant rate. The binding of bicarbonate is most affected by the mutagenesis of residues E215A, E299Q, N301D, and R303Q. The Km for ATP is most affected in the mutant enzymes R129A, R169A, Q285A, and N301D. No significant changes in the catalytic constants are observed in the mutants R82A and D207A. All of the mutations, with the exception of the N301D mutant, primarily effect the enzyme by altering the step for the phosphorylation of bicarbonate. Mutation N301D also disrupts the catalytic step involved in the phosphorylation of carbamate | Escherichia coli |
N283A | mutations of the residues E215A, N283A, E299Q, N301D, and R303Q result in proteins which are unable to synthesize carbamoyl phosphate at a significant rate. The binding of bicarbonate is most affected by the mutagenesis of residues E215A, E299Q, N301D, and R303Q. The Km for ATP is most affected in the mutant enzymes R129A, R169A, Q285A, and N301D. No significant changes in the catalytic constants are observed in the mutants R82A and D207A. All of the mutations, with the exception of the N301D mutant, primarily effect the enzyme by altering the step for the phosphorylation of bicarbonate. Mutation N301D also disrupts the catalytic step involved in the phosphorylation of carbamate | Escherichia coli |
N301D | mutations of the residues E215A, N283A, E299Q, N301D, and R303Q result in proteins which are unable to synthesize carbamoyl phosphate at a significant rate. The binding of bicarbonate is most affected by the mutagenesis of residues E215A, E299Q, N301D, and R303Q. The Km for ATP is most affected in the mutant enzymes R129A, R169A, Q285A, and N301D. No significant changes in the catalytic constants are observed in the mutants R82A and D207A. All of the mutations, with the exception of the N301D mutant, primarily effect the enzyme by altering the step for the phosphorylation of bicarbonate. Mutation N301D also disrupts the catalytic step involved in the phosphorylation of carbamate | Escherichia coli |
Q285A | mutations of the residues E215A, N283A, E299Q, N301D, and R303Q result in proteins which are unable to synthesize carbamoyl phosphate at a significant rate. The binding of bicarbonate is most affected by the mutagenesis of residues E215A, E299Q, N301D, and R303Q. The Km for ATP is most affected in the mutant enzymes R129A, R169A, Q285A, and N301D. No significant changes in the catalytic constants are observed in the mutants R82A and D207A. All of the mutations, with the exception of the N301D mutant, primarily effect the enzyme by altering the step for the phosphorylation of bicarbonate. Mutation N301D also disrupts the catalytic step involved in the phosphorylation of carbamate | Escherichia coli |
R129A | mutations of the residues E215A, N283A, E299Q, N301D, and R303Q result in proteins which are unable to synthesize carbamoyl phosphate at a significant rate. The binding of bicarbonate is most affected by the mutagenesis of residues E215A, E299Q, N301D, and R303Q. The Km for ATP is most affected in the mutant enzymes R129A, R169A, Q285A, and N301D. No significant changes in the catalytic constants are observed in the mutants R82A and D207A. All of the mutations, with the exception of the N301D mutant, primarily effect the enzyme by altering the step for the phosphorylation of bicarbonate. Mutation N301D also disrupts the catalytic step involved in the phosphorylation of carbamate | Escherichia coli |
R169A | mutations of the residues E215A, N283A, E299Q, N301D, and R303Q result in proteins which are unable to synthesize carbamoyl phosphate at a significant rate. The binding of bicarbonate is most affected by the mutagenesis of residues E215A, E299Q, N301D, and R303Q. The Km for ATP is most affected in the mutant enzymes R129A, R169A, Q285A, and N301D. No significant changes in the catalytic constants are observed in the mutants R82A and D207A. All of the mutations, with the exception of the N301D mutant, primarily effect the enzyme by altering the step for the phosphorylation of bicarbonate. Mutation N301D also disrupts the catalytic step involved in the phosphorylation of carbamate | Escherichia coli |
R303Q | mutations of the residues E215A, N283A, E299Q, N301D, and R303Q result in proteins which are unable to synthesize carbamoyl phosphate at a significant rate. The binding of bicarbonate is most affected by the mutagenesis of residues E215A, E299Q, N301D, and R303Q. The Km for ATP is most affected in the mutant enzymes R129A, R169A, Q285A, and N301D. No significant changes in the catalytic constants are observed in the mutants R82A and D207A. All of the mutations, with the exception of the N301D mutant, primarily effect the enzyme by altering the step for the phosphorylation of bicarbonate. Mutation N301D also disrupts the catalytic step involved in the phosphorylation of carbamate | Escherichia coli |
R82A | mutations of the residues E215A, N283A, E299Q, N301D, and R303Q result in proteins which are unable to synthesize carbamoyl phosphate at a significant rate. The binding of bicarbonate is most affected by the mutagenesis of residues E215A, E299Q, N301D, and R303Q. The Km for ATP is most affected in the mutant enzymes R129A, R169A, Q285A, and N301D. No significant changes in the catalytic constants are observed in the mutants R82A and D207A. All of the mutations, with the exception of the N301D mutant, primarily effect the enzyme by altering the step for the phosphorylation of bicarbonate. Mutation N301D also disrupts the catalytic step involved in the phosphorylation of carbamate | Escherichia coli |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | effect of Orn or UMP on Km-values of mutant and wild type enzyme | Escherichia coli | |
additional information | - |
additional information | kinetic constants of mutant and wild type enzymes | Escherichia coli |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
wild type and mutant enzymes | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
2 ATP + L-Gln + HCO3- | - |
Escherichia coli | 2 ADP + phosphate + L-Glu + carbamoyl phosphate | - |
? |