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Literature summary extracted from

  • Delannay, S.; Charlier, D.; Tricot, C.; Villeret, V.; Pierard, A.; Stalon, V.
    Serine 948 and threonine 1042 are crucial residues for allosteric regulation of Escherichia coli carbamoylphosphate synthetase and illustrate coupling effects of activation and inhibition pathways (1999), J. Mol. Biol., 286, 1217-1228.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
6.3.5.5 IMP
-
 Escherichia coli
6.3.5.5 L-ornithine
-
 Escherichia coli

Cloned(Commentary)

EC Number Cloned (Comment) Organism
6.3.5.5 cloning of car B wild-type and mutant enzymes Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
6.3.5.5 A182V reduced apparent affinity for HCO3-, sensitivity toward UMP is unchanched in comparison to wild-type enzyme Escherichia coli
6.3.5.5 A182V/S948F mutant is insensitive towards pyrimidine and purine nucleosides, activation by ornithine, although the affinity for this ligand is fivefold reduced in comparison to wild-type enzyme Escherichia coli
6.3.5.5 G824D strongly reduced affinity for ornithine in comparison to wild-type enzyme Escherichia coli
6.3.5.5 P165S reduced apparent affinity for HCO3-, sensitivity toward UMP is increased in comparison to wild-type enzyme Escherichia coli
6.3.5.5 P170L reduced apparent affinity for HCO3-, sensitivity toward UMP is increased in comparison to wild-type enzyme Escherichia coli
6.3.5.5 P360L UMP still inhibits the activity of the mutant enzyme, 30fold reduced affinity for ornithine and 20fold reduced affinity for IMP in comparison to wild-type enzyme Escherichia coli
6.3.5.5 S743N minor modification of kinetic parameters in comparison to wild-type enzyme Escherichia coli
6.3.5.5 S743N/G824D strongly reduced affinity for ornithine in comparison to wild-type enzyme Escherichia coli
6.3.5.5 S948F mutant enzyme is unsensitive to UMP and IMP, but is still activated by ornithine, although to a reduced extent Escherichia coli
6.3.5.5 T1042I greatly reduced activation by ornithine, the affinities for both UMP and IMP are reduced in comparison to wild-type enzyme in comparison to wild-type enzyme Escherichia coli
6.3.5.5 T1042I mutation reduces activation by ornithine, the mutated enzyme is still sensitive to UMP and IMP Escherichia coli
6.3.5.5 T800F reduced affinity for ornithine, increased sensitivity for UMP in comparison to wild-type enzyme Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
6.3.5.5 UMP
-
 Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
6.3.5.5 0.12
-
 L-glutamine pH 7.5, 37°C, value of wild-type enzyme in comparison to values of mutant enzymes Escherichia coli
6.3.5.5 1.2
-
 HCO3- pH 7.5, 37°C, value of wild-type enzyme in comparison to values of mutant enzymes 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 enzyme is a key enzyme in the pyrimidine nucleotide and arginine biosynthetic pathways 2 ADP + phosphate + L-Glu + carbamoyl phosphate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
6.3.5.5 Escherichia coli
-
 K-12
-

Purification (Commentary)

EC Number Purification (Comment) Organism
6.3.5.5 recombinant wild-type and mutant enzymes 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 two residues, Ser948 and Thr1042, appear crucial for allosteric regulation of enzyme Escherichia coli
a

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
-
 ?
6.3.5.5 2 ATP + L-Gln + HCO3- enzyme is a key enzyme in the pyrimidine nucleotide and arginine biosynthetic pathways Escherichia coli 2 ADP + phosphate + L-Glu + carbamoyl phosphate
-
 ?

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
6.3.5.5 0.005
-
 UMP pH 7.5, 37°C, value of wild-type enzyme in comparison to values of mutant enzymes Escherichia coli