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Literature summary for 2.4.2.3 extracted from
- Uridine phosphorylase from Trypanosoma cruzi: kinetic and chemical mechanisms (2011), Biochemistry, 50, 9158-9166.
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| alpha-D-ribose 1-phosphate | product inhibition, noncompetitive with respect to uridine and phosphate | Trypanosoma cruzi |  |
| Uracil | product inhibition, oncompetitive with respect to uridine and phosphate | Trypanosoma cruzi | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Trypanosoma cruzi | - |
- |
- |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| uridine + phosphate = uracil + alpha-D-ribose 1-phosphate | steady-state random kinetic mechanism. Reaction follows an ANDN/SN2 mechanism where chemistry contributes significantly to the overall rate-limiting step of the reaction. No kinetically significant proton transfer step is involved at the transition state. Proton transfer to neutralize the leaving group is not part of transition state formation, consistent with an enzyme-stabilized anionic uracil as the leaving group. Kinetic analysis as a function of pH indicates one protonated group essential for catalysis and for substrate binding | Trypanosoma cruzi |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| uridine + phosphate | - |
Trypanosoma cruzi | uracil + alpha-D-ribose 1-phosphate | - |
? | |
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