Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Fresquet, V.; Mora, P.; Rochera, L.; Ramon-Maiques, S.; Rubio, V.; Cervera, J.
    Site-directed mutagenesis of the regulatory domain of Escherichia coli carbamoyl phosphate synthetase identifies crucial residues for allosteric regulation and for transduction of the regulatory signals (2000), J. Mol. Biol., 299, 979-991.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
6.3.5.5 IMP the IMP activator and the UMP inhibitor bind to the same site on the enzyme Escherichia coli
6.3.5.5 ornithine
-
 Escherichia coli

Cloned(Commentary)

EC Number Cloned (Comment) Organism
6.3.5.5 expression in Echerichia coli Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
6.3.5.5 G1008A mutation abolishs IMP activation and UMP inhibition in comparison to wild-type enzyme Escherichia coli
6.3.5.5 G997A mutation abolishs IMP activation and UMP inhibition in comparison to wild-type enzyme Escherichia coli
6.3.5.5 H995A mutation has little effect on enzyme activity in comparison to wild-type enzyme Escherichia coli
6.3.5.5 K1061A mutation abolishs IMP activation and UMP inhibition in comparison to wild-type enzyme Escherichia coli
6.3.5.5 K954A mutation has little effect on enzyme activity in comparison to wild-type enzyme Escherichia coli
6.3.5.5 K993A mutation reduces enzyme activity in comparison to wild-type enzyme Escherichia coli
6.3.5.5 K993W mutation has little effect on enzyme activity in comparison to wild-type enzyme Escherichia coli
6.3.5.5 K993W/H995A mutation abolishs IMP activation and UMP inhibition in comparison to wild-type enzyme Escherichia coli
6.3.5.5 L990A mutation abolishs IMP activation and UMP inhibition in comparison to wild-type enzyme Escherichia coli
6.3.5.5 R1020A mutation has little effect on enzyme activity in comparison to wild-type enzyme Escherichia coli
6.3.5.5 R1021A mutation has little effect on enzyme activity in comparison to wild-type enzyme Escherichia coli
6.3.5.5 S948A mutation has little effect on enzyme activity in comparison to wild-type enzyme Escherichia coli
6.3.5.5 T974A mutation abolishs IMP activation and UMP inhibition in comparison to wild-type enzyme Escherichia coli
6.3.5.5 V991A mutation has little effect on enzyme activity in comparison to wild-type enzyme Escherichia coli
6.3.5.5 V994A mutation reduces enzyme activity in comparison to wild-type enzyme Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
6.3.5.5 UMP the IMP activator and the UMP inhibitor bind to the same site on the enzyme Escherichia coli

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
6.3.5.5 41400
-
 1 * 41400 + 1 * 117700, the large subunit catalyses the carbamoyl phosphate synthesis from ammonia in three steps, and binds the effectors in its 15000 domain Escherichia coli
6.3.5.5 117700
-
 1 * 41400 + 1 * 117700, the large subunit catalyses the carbamoyl phosphate synthesis from ammonia in three steps, and binds the effectors in its 15000 domain 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
-
 ?
6.3.5.5 2 ATP + L-Gln + HCO3- Escherichia coli L814 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
-
 L814
-
6.3.5.5 Escherichia coli L814
-
 L814
-

Purification (Commentary)

EC Number Purification (Comment) Organism
6.3.5.5 recombinant wild-type and mutant enzymes Escherichia coli

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
-
 ?
6.3.5.5 2 ATP + L-Gln + HCO3-
-
 Escherichia coli L814 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 L814 2 ADP + phosphate + L-Glu + carbamoyl phosphate
-
 ?
6.3.5.5 2 ATP + NH4+ + HCO3-
-
 Escherichia coli 2 ADP + phosphate + carbamoyl phosphate
-
 ?
6.3.5.5 2 ATP + NH4+ + HCO3-
-
 Escherichia coli L814 2 ADP + phosphate + carbamoyl phosphate
-
 ?

Subunits

EC Number Subunits Comment Organism
6.3.5.5 dimer 1 * 41400 + 1 * 117700, the large subunit catalyses the carbamoyl phosphate synthesis from ammonia in three steps, and binds the effectors in its 15000 domain Escherichia coli

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
6.3.5.5 0.0018
-
 UMP pH 8.0, 37°C, wild-type enzyme in comparison to mutant enzymes Escherichia coli