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Literature summary for 2.4.2.9 extracted from
- Kinetic studies of the uracil phosphoribosyltransferase reaction catalyzed by the Bacillus subtilis pyrimidine attenuation regulatory protein PyrR (2003), J. Biol. Chem., 278, 6921-6927.
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| diphosphate | product inhibition forward reaction | Bacillus subtilis |  |
| UMP | product inhibition, forward reaction | Bacillus subtilis | |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.068 | - |
5-phospho-alpha-D-ribose 1-diphosphate | - |
Bacillus subtilis | |
| 0.13 | - |
UMP | - |
Bacillus subtilis | |
| 0.159 | - |
Uracil | - |
Bacillus subtilis | |
| 1 | - |
diphosphate | - |
Bacillus subtilis | |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | - |
Bacillus subtilis | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bacillus subtilis | - |
PyrR protein | - |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| UMP + diphosphate = uracil + 5-phospho-alpha-D-ribose 1-diphosphate | ping pong steady state kinetic pattern, ordered bi-bi mechanism, model, no formation of the phosphoribosyl-enzyme intermediate predicted by classic ping pong kinetics | Bacillus subtilis |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | no catalysis of exchange reaction between uracil-UMP and diphosphate-5-phospho-alpha-D-ribose 1-diphosphate | Bacillus subtilis | ? | - |
? | |
| uracil + 5-phospho-alpha-D-ribose 1-diphosphate | equilibrium lies far in the direction of UMP formation | Bacillus subtilis | UMP + diphosphate | - |
r | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| More | PyrR protein is a bifunctional protein, that primarily regulates the expression of pyrimidine biosynthetic pyr genes, but also catalyses the uracil phosphoribosyltransferase reaction, little amino acid sequence similarities to other bacterial UPRTases | Bacillus subtilis |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
assay at | Bacillus subtilis |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.0015 | - |
UMP | reverse reaction | Bacillus subtilis | |
| 5.1 | - |
Uracil | forward reaction | Bacillus subtilis | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8.7 | - |
assay at | Bacillus subtilis |
Ki Value [mM]
| Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | product inhibition pattern | Bacillus subtilis |
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