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Literature summary for 6.3.5.5 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
Search for more literature for 6.3.5.5

Activating Compound

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

Cloned(Commentary)

Cloned (Comment) Organism
expression in Echerichia coli Escherichia coli

Protein Variants

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

Inhibitors

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

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
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
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)

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
-
 ?
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

Organism UniProt Comment Textmining
Escherichia coli
-
 L814
-
Escherichia coli L814
-
 L814
-

Purification (Commentary)

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

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
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]

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