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Literature summary for 6.3.5.5 extracted from
- carbamyl phosphate synthetase (glutamine-utilizing) from Escherichia coli (1985), Methods Enzymol., 113, 305-326.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| GTP | enhances activity | Escherichia coli |  |
| ITP | enhances activity | Escherichia coli | |
| NEM | 250fold activation of glutaminase activity. Irreversible inactivation of synthetase activity | Escherichia coli | |
| Orn | activates | Escherichia coli | |
| XMP | enhances activity | Escherichia coli | |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
- |
Escherichia coli |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| 6-diazo-5-oxonorleucine | selective inactivation of Gln-dependent activity | Escherichia coli | |
| Alkyl hydrazines | inhibits Gln-dependent activity, but not NH4+-dependent activity | Escherichia coli | |
| azaserine | selective inactivation of Gln-dependent activity | Escherichia coli | |
| H2O2 | 0.2 mM, inhibits Gln-dependent activity. No effect on the activity with NH4+ in carbamoyl-phosphate synthase reaction | Escherichia coli | |
| hydroxylamine | inhibits Gln-dependent activity, but not NH4+-dependent activity | Escherichia coli | |
| L-2-Amino-4-oxo-5-chloropentanoate | selective inactivation of Gln-dependent activity | Escherichia coli | |
| NEM | irreversible inactivation of synthetase activity. Increase of glutaminase activity | Escherichia coli | |
| potassium cyanate | inhibits Gln-dependent activity, but not NH4+-dependent activity | Escherichia coli | |
| UDP | inhibits to a lesser extent than UMP | Escherichia coli | |
| UMP | phosphate increases inhibition | Escherichia coli | |
| UTP | inhibits to a lesser extent than UMP | Escherichia coli | |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.38 | - |
L-Gln | - |
Escherichia coli | |
| 93 | - |
NH4+ | - |
Escherichia coli | |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| K+ | optimal concentration: 0.1 M | Escherichia coli | |
| NH4+ | activates | Escherichia coli | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 40000 | - |
1 * 40000 + 1 * 130000, SDS-PAGE | Escherichia coli |
| 130000 | - |
1 * 40000 + 1 * 130000, SDS-PAGE | Escherichia coli |
| 163000 | - |
sedimentation equilibrium ultracentrifugation | Escherichia coli |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
| Escherichia coli B / ATCC 11303 | - |
- |
- |
Oxidation Stability
| Oxidation Stability | Organism |
|---|---|
| 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)
| Purification (Comment) | Organism |
|---|---|
- |
Escherichia coli |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| additional information | - |
- |
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- | - |
Escherichia coli B / ATCC 11303 | 2 ADP + phosphate + L-Glu + carbamoyl phosphate | - |
? | |
| 2 ATP + NH4+ + HCO3- | - |
Escherichia coli | 2 ADP + phosphate + carbamoyl phosphate | - |
? | |
| 2 ATP + NH4+ + HCO3- | - |
Escherichia coli B / ATCC 11303 | 2 ADP + phosphate + carbamoyl phosphate | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| dimer | 1 * 40000 + 1 * 130000, SDS-PAGE | Escherichia coli |
| 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
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.8 | 8.2 | - |
Escherichia coli |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| AMP | enhances activity | Escherichia coli | |
| GDP | enhances activity | Escherichia coli | |
| GMP | enhances activity | Escherichia coli | |
| IDP | enhances activity | Escherichia coli | |
| IMP | phosphate decreases activation | Escherichia coli | |
| IMP | stimulates | Escherichia coli | |
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