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Literature summary extracted from

  • Kaseman, D.S.; Meister, A.
    carbamyl phosphate synthetase (glutamine-utilizing) from Escherichia coli (1985), Methods Enzymol., 113, 305-326.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
6.3.5.5 GTP enhances activity Escherichia coli
6.3.5.5 ITP enhances activity Escherichia coli
6.3.5.5 NEM 250fold activation of glutaminase activity. Irreversible inactivation of synthetase activity Escherichia coli
6.3.5.5 Orn activates Escherichia coli
6.3.5.5 XMP enhances activity Escherichia coli

Cloned(Commentary)

EC Number Cloned (Comment) Organism
6.3.5.5
-
 Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
6.3.5.5 6-diazo-5-oxonorleucine selective inactivation of Gln-dependent activity Escherichia coli
6.3.5.5 Alkyl hydrazines inhibits Gln-dependent activity, but not NH4+-dependent activity Escherichia coli
6.3.5.5 azaserine selective inactivation of Gln-dependent activity Escherichia coli
6.3.5.5 H2O2 0.2 mM, inhibits Gln-dependent activity. No effect on the activity with NH4+ in carbamoyl-phosphate synthase reaction Escherichia coli
6.3.5.5 hydroxylamine inhibits Gln-dependent activity, but not NH4+-dependent activity Escherichia coli
6.3.5.5 L-2-Amino-4-oxo-5-chloropentanoate selective inactivation of Gln-dependent activity Escherichia coli
6.3.5.5 NEM irreversible inactivation of synthetase activity. Increase of glutaminase activity Escherichia coli
6.3.5.5 potassium cyanate inhibits Gln-dependent activity, but not NH4+-dependent activity Escherichia coli
6.3.5.5 UDP inhibits to a lesser extent than UMP Escherichia coli
6.3.5.5 UMP phosphate increases inhibition Escherichia coli
6.3.5.5 UTP inhibits to a lesser extent than UMP Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
6.3.5.5 0.38
-
 L-Gln
-
 Escherichia coli
6.3.5.5 93
-
 NH4+
-
 Escherichia coli

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
6.3.5.5 K+ optimal concentration: 0.1 M Escherichia coli
6.3.5.5 NH4+ activates Escherichia coli

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
6.3.5.5 40000
-
 1 * 40000 + 1 * 130000, SDS-PAGE Escherichia coli
6.3.5.5 130000
-
 1 * 40000 + 1 * 130000, SDS-PAGE Escherichia coli
6.3.5.5 163000
-
 sedimentation equilibrium ultracentrifugation Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
6.3.5.5 Escherichia coli
-
-
-
6.3.5.5 Escherichia coli B / ATCC 11303
-
-
-

Oxidation Stability

EC Number Oxidation Stability Organism
6.3.5.5 Gln-dependent function of carbamoyl-phosphate synthase is inactivated by incubating the enzyme in air with low concentrations of dithiothreitol, glutathione, Cys, homocysteine, or 2-mercaptoethanol Escherichia coli

Purification (Commentary)

EC Number Purification (Comment) Organism
6.3.5.5
-
 Escherichia coli

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
6.3.5.5 additional information
-
-
 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-
-
 Escherichia coli B / ATCC 11303 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 B / ATCC 11303 2 ADP + phosphate + carbamoyl phosphate
-
 ?

Subunits

EC Number Subunits Comment Organism
6.3.5.5 dimer 1 * 40000 + 1 * 130000, SDS-PAGE Escherichia coli
6.3.5.5 More enzyme exists in monomer, dimer, and higher oligomeric forms, which are associated with its regulation by allosteric effectors. In barbital buffer the enzyme is present as a monomer. In sodium phosphate buffer, the enzyme exists as a partially dissociating dimer. In presence of phosphate and a positive allosteric effector, the maximum association state of the enzyme is a tetramer. UMP promotes conversion to a dimer Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
6.3.5.5 7.8 8.2
-
 Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
6.3.5.5 AMP enhances activity Escherichia coli
6.3.5.5 GDP enhances activity Escherichia coli
6.3.5.5 GMP enhances activity Escherichia coli
6.3.5.5 IDP enhances activity Escherichia coli
6.3.5.5 IMP phosphate decreases activation Escherichia coli
6.3.5.5 IMP stimulates Escherichia coli