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Literature summary extracted from

  • Czerwinski, R.M.; Mareya, S.M.; Raushel, F.M.
    Regulatory changes in the control of carbamoyl phosphate synthetase induced by truncation and mutagenesis of the allosteric binding domain (1995), Biochemistry, 34, 13920-13927.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
6.3.5.5 DELTA119 truncation mutant DELTA14, with a removal of 14 amino acids at the carboxy terminus of the large subunit shows a 40fold decrease in Gln-dependent ATPase activity. Similar losses in activity are observed for the DELTA50, DELTA65, DELTA91, and DELTA119 mutant proteins. However formation of carbamoyl phosphate is detected even after the deletion of 119 amino acids from the carboxy-terminal end of the large subunit. No allosteric effects are observed in the presence of Orn even after the removal of the last 119 amino acids from the large subunit of CPS. Mutant enzymes G921V and G921I are unstable and are defective for the synthesis of carbamoyl phosphate. The T977A mutant is not regulated by UMP, but the full allosteric effect is observed with Orn. The R1030A and R1031A mutants enzymes exhibit wild type properties, mutant G921A shows no alteration in any of the allosteric properties. Mutant N1015A cannot be purified Escherichia coli
6.3.5.5 DELTA14 truncation mutant DELTA14, with a removal of 14 amino acids at the carboxy terminus of the large subunit shows a 40fold decrease in Gln-dependent ATPase activity. Similar losses in activity are observed for the DELTA50, DELTA65, DELTA91, and DELTA119 mutant proteins. However formation of carbamoyl phosphate is detected even after the deletion of 119 amino acids from the carboxy-terminal end of the large subunit. No allosteric effects are observed in the presence of Orn even after the removal of the last 119 amino acids from the large subunit of CPS. Mutant enzymes G921V and G921I are unstable and are defective for the synthesis of carbamoyl phosphate. The T977A mutant is not regulated by UMP, but the full allosteric effect is observed with Orn. The R1030A and R1031A mutants enzymes exhibit wild type properties, mutant G921A shows no alteration in any of the allosteric properties. Mutant N1015A cannot be purified Escherichia coli
6.3.5.5 DELTA50 truncation mutant DELTA14, with a removal of 14 amino acids at the carboxy terminus of the large subunit shows a 40fold decrease in Gln-dependent ATPase activity. Similar losses in activity are observed for the DELTA50, DELTA65, DELTA91, and DELTA119 mutant proteins. However formation of carbamoyl phosphate is detected even after the deletion of 119 amino acids from the carboxy-terminal end of the large subunit. No allosteric effects are observed in the presence of Orn even after the removal of the last 119 amino acids from the large subunit of CPS. Mutant enzymes G921V and G921I are unstable and are defective for the synthesis of carbamoyl phosphate. The T977A mutant is not regulated by UMP, but the full allosteric effect is observed with Orn. The R1030A and R1031A mutants enzymes exhibit wild type properties, mutant G921A shows no alteration in any of the allosteric properties. Mutant N1015A cannot be purified Escherichia coli
6.3.5.5 DELTA65 truncation mutant DELTA14, with a removal of 14 amino acids at the carboxy terminus of the large subunit shows a 40fold decrease in Gln-dependent ATPase activity. Similar losses in activity are observed for the DELTA50, DELTA65, DELTA91, and DELTA119 mutant proteins. However formation of carbamoyl phosphate is detected even after the deletion of 119 amino acids from the carboxy-terminal end of the large subunit. No allosteric effects are observed in the presence of Orn even after the removal of the last 119 amino acids from the large subunit of CPS. Mutant enzymes G921V and G921I are unstable and are defective for the synthesis of carbamoyl phosphate. The T977A mutant is not regulated by UMP, but the full allosteric effect is observed with Orn. The R1030A and R1031A mutants enzymes exhibit wild type properties, mutant G921A shows no alteration in any of the allosteric properties. Mutant N1015A cannot be purified Escherichia coli
6.3.5.5 DELTA91 truncation mutant DELTA14, with a removal of 14 amino acids at the carboxy terminus of the large subunit shows a 40fold decrease in Gln-dependent ATPase activity. Similar losses in activity are observed for the DELTA50, DELTA65, DELTA91, and DELTA119 mutant proteins. However formation of carbamoyl phosphate is detected even after the deletion of 119 amino acids from the carboxy-terminal end of the large subunit. No allosteric effects are observed in the presence of Orn even after the removal of the last 119 amino acids from the large subunit of CPS. Mutant enzymes G921V and G921I are unstable and are defective for the synthesis of carbamoyl phosphate. The T977A mutant is not regulated by UMP, but the full allosteric effect is observed with Orn. The R1030A and R1031A mutants enzymes exhibit wild type properties, mutant G921A shows no alteration in any of the allosteric properties. Mutant N1015A cannot be purified Escherichia coli
6.3.5.5 G921A truncation mutant DELTA14, with a removal of 14 amino acids at the carboxy terminus of the large subunit shows a 40fold decrease in Gln-dependent ATPase activity. Similar losses in activity are observed for the DELTA50, DELTA65, DELTA91, and DELTA119 mutant proteins. However formation of carbamoyl phosphate is detected even after the deletion of 119 amino acids from the carboxy-terminal end of the large subunit. No allosteric effects are observed in the presence of Orn even after the removal of the last 119 amino acids from the large subunit of CPS. Mutant enzymes G921V and G921I are unstable and are defective for the synthesis of carbamoyl phosphate. The T977A mutant is not regulated by UMP, but the full allosteric effect is observed with Orn. The R1030A and R1031A mutants enzymes exhibit wild type properties, mutant G921A shows no alteration in any of the allosteric properties. Mutant N1015A cannot be purified Escherichia coli
6.3.5.5 G921I truncation mutant DELTA14, with a removal of 14 amino acids at the carboxy terminus of the large subunit shows a 40fold decrease in Gln-dependent ATPase activity. Similar losses in activity are observed for the DELTA50, DELTA65, DELTA91, and DELTA119 mutant proteins. However formation of carbamoyl phosphate is detected even after the deletion of 119 amino acids from the carboxy-terminal end of the large subunit. No allosteric effects are observed in the presence of Orn even after the removal of the last 119 amino acids from the large subunit of CPS. Mutant enzymes G921V and G921I are unstable and are defective for the synthesis of carbamoyl phosphate. The T977A mutant is not regulated by UMP, but the full allosteric effect is observed with Orn. The R1030A and R1031A mutants enzymes exhibit wild type properties, mutant G921A shows no alteration in any of the allosteric properties. Mutant N1015A cannot be purified Escherichia coli
6.3.5.5 G921V truncation mutant DELTA14, with a removal of 14 amino acids at the carboxy terminus of the large subunit shows a 40fold decrease in Gln-dependent ATPase activity. Similar losses in activity are observed for the DELTA50, DELTA65, DELTA91, and DELTA119 mutant proteins. However formation of carbamoyl phosphate is detected even after the deletion of 119 amino acids from the carboxy-terminal end of the large subunit. No allosteric effects are observed in the presence of Orn even after the removal of the last 119 amino acids from the large subunit of CPS. Mutant enzymes G921V and G921I are unstable and are defective for the synthesis of carbamoyl phosphate. The T977A mutant is not regulated by UMP, but the full allosteric effect is observed with Orn. The R1030A and R1031A mutants enzymes exhibit wild type properties, mutant G921A shows no alteration in any of the allosteric properties. Mutant N1015A cannot be purified Escherichia coli
6.3.5.5 N1015A truncation mutant DELTA14, with a removal of 14 amino acids at the carboxy terminus of the large subunit shows a 40fold decrease in Gln-dependent ATPase activity. Similar losses in activity are observed for the DELTA50, DELTA65, DELTA91, and DELTA119 mutant proteins. However formation of carbamoyl phosphate is detected even after the deletion of 119 amino acids from the carboxy-terminal end of the large subunit. No allosteric effects are observed in the presence of Orn even after the removal of the last 119 amino acids from the large subunit of CPS. Mutant enzymes G921V and G921I are unstable and are defective for the synthesis of carbamoyl phosphate. The T977A mutant is not regulated by UMP, but the full allosteric effect is observed with Orn. The R1030A and R1031A mutants enzymes exhibit wild type properties, mutant G921A shows no alteration in any of the allosteric properties. Mutant N1015A cannot be purified Escherichia coli
6.3.5.5 R1030A truncation mutant DELTA14, with a removal of 14 amino acids at the carboxy terminus of the large subunit shows a 40fold decrease in Gln-dependent ATPase activity. Similar losses in activity are observed for the DELTA50, DELTA65, DELTA91, and DELTA119 mutant proteins. However formation of carbamoyl phosphate is detected even after the deletion of 119 amino acids from the carboxy-terminal end of the large subunit. No allosteric effects are observed in the presence of Orn even after the removal of the last 119 amino acids from the large subunit of CPS. Mutant enzymes G921V and G921I are unstable and are defective for the synthesis of carbamoyl phosphate. The T977A mutant is not regulated by UMP, but the full allosteric effect is observed with Orn. The R1030A and R1031A mutants enzymes exhibit wild type properties, mutant G921A shows no alteration in any of the allosteric properties. Mutant N1015A cannot be purified Escherichia coli
6.3.5.5 R1031A truncation mutant DELTA14, with a removal of 14 amino acids at the carboxy terminus of the large subunit shows a 40fold decrease in Gln-dependent ATPase activity. Similar losses in activity are observed for the DELTA50, DELTA65, DELTA91, and DELTA119 mutant proteins. However formation of carbamoyl phosphate is detected even after the deletion of 119 amino acids from the carboxy-terminal end of the large subunit. No allosteric effects are observed in the presence of Orn even after the removal of the last 119 amino acids from the large subunit of CPS. Mutant enzymes G921V and G921I are unstable and are defective for the synthesis of carbamoyl phosphate. The T977A mutant is not regulated by UMP, but the full allosteric effect is observed with Orn. The R1030A and R1031A mutants enzymes exhibit wild type properties, mutant G921A shows no alteration in any of the allosteric properties. Mutant N1015A cannot be purified Escherichia coli
6.3.5.5 T977A truncation mutant DELTA14, with a removal of 14 amino acids at the carboxy terminus of the large subunit shows a 40fold decrease in Gln-dependent ATPase activity. Similar losses in activity are observed for the DELTA50, DELTA65, DELTA91, and DELTA119 mutant proteins. However formation of carbamoyl phosphate is detected even after the deletion of 119 amino acids from the carboxy-terminal end of the large subunit. No allosteric effects are observed in the presence of Orn even after the removal of the last 119 amino acids from the large subunit of CPS. Mutant enzymes G921V and G921I are unstable and are defective for the synthesis of carbamoyl phosphate. The T977A mutant is not regulated by UMP, but the full allosteric effect is observed with Orn. The R1030A and R1031A mutants enzymes exhibit wild type properties, mutant G921A shows no alteration in any of the allosteric properties. Mutant N1015A cannot be purified 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 kinetic constants of mutant and wild type enzymes Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
6.3.5.5 Escherichia coli
-
 wild type and mutant enzymes
-

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
-
 ?