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Literature summary extracted from

  • Guy, H.I.; Schmidt, B.; Herve, G.; Evans, D.R.
    Pressure-induced dissociation of carbamoyl-phosphate synthetase domains. The catalytically active form is dimeric (1998), J. Biol. Chem., 273, 14172-14178.
    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

Inhibitors

EC Number Inhibitors Comment Organism Structure
6.3.5.5 UMP
-
 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
-
-
-

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 effects of pressure on the partial reactions, study of the function of monomers of enzyme domains under conditions of pressure-induced dissociation 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
-
 ?

Subunits

EC Number Subunits Comment Organism
6.3.5.5 dimer The enzyme consists of an amidotransferase domain or subunit, GLN, 40000 Da, that hydrolyzes glutamine and transfers the ammonia to the synthetase component, CPS, 120000 Da, where the biosynthetic reaction occurs. The CPS domain is composed of two homologous subdomains, CPS.A and CPS.B, that catalyse different ATP-dependent reactions involved in the carbamoyl phosphate synthesis. The CPS.A and CPS.B monomers could each catalyse all of the partial reactions, but catalysis of the overall synthesis of carbamoyl phosphate requires a dimer composed of two of the equivalent domains. Escherichia coli