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Literature summary for 6.3.5.5 extracted from
- Genetic identification of essential indels and domains in carbamoyl phosphate synthetase II of Toxoplasma gondii (2008), Int. J. Parasitol., 39, 533-539.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| additional information | CPSII GATase domain as well as the C-terminal allosteric regulatory domain are essential, critical dependence on the apicomplexan CPSII GATase domain in vivo, overview | Toxoplasma gondii |
Application
| Application | Comment | Organism |
|---|---|---|
| drug development | CPSII is a potential parasite-selective target for drug development | Toxoplasma gondii |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| construction and expression of a functional minigene of CPSII for functional complementation of mutants, overview | Toxoplasma gondii |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| C345A | site-directed mutagenesis of an essential catalytic triad residue of the GATase domain, the mutation completely abolishes complementation activity and GATase activity | Toxoplasma gondii |
| additional information | disruption of Toxoplasma gondii CPSII induces a severe uracil auxotrophy with no detectable parasite replication in vitro and complete attenuation of virulence in mice. A CPSII cDNA minigene efficiently complements the uracil auxotrophy of CPSII-deficient mutants, restoring parasite growth and virulence, engineered mutations within, or proximal to, but the catalytic triad of the N-terminal glutamine amidotransferase domain inactivates the complementation activity of CPSII and demonstrates a critical dependence on the apicomplexan CPSII GATase domain in vivo | Toxoplasma gondii |
| N348A | site-directed mutagenesis, the mutation reduces complementation activity, GATase activity and the initial growth rate, but the N348A mutant exhibits the high virulence phenotype of the parental RH strain in C57Bl/6 mice | Toxoplasma gondii |
| N348R | site-directed mutagenesis, the mutation completely abolishes complementation activity and GATase activity | Toxoplasma gondii |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | - |
Toxoplasma gondii |  |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + L-glutamine + HCO3- + H2O | Toxoplasma gondii | allosteric regulation and CPSII regulatory domains, overview | ADP + phosphate + L-glutamate + carbamoyl phosphate | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Toxoplasma gondii | - |
strains cps1-1 and RH | - |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| tachyzoite | maintained in human foreskin fibroblasts | Toxoplasma gondii | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + L-glutamine + HCO3- + H2O | - |
Toxoplasma gondii | ADP + phosphate + L-glutamate + carbamoyl phosphate | - |
? | |
| ATP + L-glutamine + HCO3- + H2O | allosteric regulation and CPSII regulatory domains, overview | Toxoplasma gondii | ADP + phosphate + L-glutamate + carbamoyl phosphate | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| carbamoyl phosphate synthetase II | - |
Toxoplasma gondii |
| CPSII | - |
Toxoplasma gondii |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| ATP | - |
Toxoplasma gondii | |
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Release 2023.1 (January 2023)
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