Activating Compound | Comment | Organism | Structure |
---|---|---|---|
IMP | - |
Escherichia coli | |
L-ornithine | - |
Escherichia coli |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
UMP | - |
Escherichia coli |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
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 | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Purification (Comment) | Organism |
---|---|
recombinant wild-type and mutant enzymes | Escherichia coli |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
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 |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
2 ATP + L-Gln + HCO3- | - |
Escherichia coli | 2 ADP + phosphate + L-Glu + carbamoyl phosphate | - |
? | |
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 | Comment | Organism |
---|---|---|
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 |