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Literature summary for 6.3.4.2 extracted from
- Mutational analysis of conserved glycine residues 142, 143 and 146 reveals Gly(142) is critical for tetramerization of CTP synthase from Escherichia coli (2008), Biochem. J., 412, 113-121.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| GTP | required, activates | Escherichia coli |  |
| additional information | binding of the substrates ATP and UTP, or the product CTP, promotes oligomerization of CTPS from inactive dimers to active tetramers, Gly142 is critical for nucleotide-dependent oligomerization of CTPS to active tetramers | Escherichia coli |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| G142A | site-directed mutagenesis, inactive mutant with both ammonia and glutamine | Escherichia coli |
| G143A | site-directed mutagenesis, kcat/Km for ammonia-dependent and glutamine-dependent CTP formation by mutant G143A are reduced by 22fold and 16fold, respectively, compared to the wild-type enzyme. The mutant is able to form active tetramers in the presence of ATP and UTP | Escherichia coli |
| G146A | site-directed mutagenesis, kcat/Km for ammonia-dependent and glutamine-dependent CTP formation by mutant G143A are reduced by 1.4fold and 1.8fold, respectively, compared to the wild-type enzyme. The mutant is able to form active tetramers in the presence of ATP and UTP | Escherichia coli |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | kinetics of wild-type and mutants | Escherichia coli |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | - |
Escherichia coli | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + UTP + L-glutamine | Escherichia coli | - |
ADP + phosphate + CTP + L-glutamate | - |
? | |
| ATP + UTP + NH3 | Escherichia coli | - |
ADP + phosphate + CTP | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | P0A7E5 | - |
- |
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. |
|---|---|---|---|---|---|---|
| ATP + UTP + L-glutamine | - |
Escherichia coli | ADP + phosphate + CTP + L-glutamate | - |
? | |
| ATP + UTP + L-glutamine | CTPS catalyses the ATP-dependent formation of CTP from UTP using either ammonia or L-glutamine as the nitrogen source | Escherichia coli | ADP + phosphate + CTP + L-glutamate | - |
? | |
| ATP + UTP + NH3 | - |
Escherichia coli | ADP + phosphate + CTP | - |
? | |
| ATP + UTP + NH3 | CTPS catalyses the ATP-dependent formation of CTP from UTP using either ammonia or L-glutamine as the nitrogen source | Escherichia coli | ADP + phosphate + CTP | - |
? | |
| additional information | UTP- and CTP-binding structures, overview | Escherichia coli | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | binding of the substrates ATP and UTP, or the product CTP, promotes oligomerization of CTPS from inactive dimers to active tetramers, Gly142 is critical for nucleotide-dependent oligomerization of CTPS to active tetramers. Oligomerization of Gly mutant enzymes, overview | Escherichia coli |
| tetramer | conserved Gly142 is critical for tetramerization, overview | Escherichia coli |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| CTP synthase | - |
Escherichia coli |
| CTPS | - |
Escherichia coli |
| cytidine 5'-triphosphate synthase | - |
Escherichia coli |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
assay at | Escherichia coli |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.08 | - |
UTP | pH 8.0, 37°C, mutant G142A with L-glutamine, in presence of 0.25 mM GTP | Escherichia coli | |
| 0.67 | - |
UTP | pH 8.0, 37°C, mutant G143A with L-glutamine, in presence of 0.25 mM GTP | Escherichia coli | |
| 4.2 | - |
UTP | pH 8.0, 37°C, mutant G146A with L-glutamine, in presence of 0.25 mM GTP | Escherichia coli | |
| 5 | - |
UTP | pH 8.0, 37°C, wild-type enzyme with L-glutamine, in presence of 0.25 mM GTP | Escherichia coli | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8 | - |
assay at | Escherichia coli |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| ATP | dependent on | Escherichia coli | |
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