KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | detailed kinetic analysis, isothermal titration calorimetry, the double Theorell-Chance mechanism yields a steady-state rate equation indistinguishable in form from the observed classical ping-pong bi-bi kinetics, steady-state kinetics, overview | Saccharomyces cerevisiae |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | required for substrate binding | Saccharomyces cerevisiae |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
orotidine 5-phosphate + diphosphate | Saccharomyces cerevisiae | - |
orotate + 5-phospho-alpha-D-ribose 1-diphosphate | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Saccharomyces cerevisiae | - |
- |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
orotidine 5'-phosphate + diphosphate = orotate + 5-phospho-alpha-D-ribose 1-diphosphate | reaction scheme, half-of-sites binding of orotidine 5-phosphate and alpha-D-5-phosphorylribose 1-diphosphate to the enzyme supports an alternative variant of the Theorell-Chance mechanism with alternating site catalysis, in addition to a ping-pong bi-bi kinetic mechanism, overview | Saccharomyces cerevisiae |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | half-of-sites binding of orotidine 5-phosphate and alpha-D-5-phosphorylribose 1-diphosphate to the enzyme supports an alternative variant of the Theorell-Chance mechanism with alternating site catalysis, overview | Saccharomyces cerevisiae | ? | - |
? | |
orotidine 5-phosphate + diphosphate | - |
Saccharomyces cerevisiae | orotate + 5-phospho-alpha-D-ribose 1-diphosphate | - |
? | |
orotidine 5-phosphate + diphosphate | the compounds bind very tightly to the enzyme in a Mg2+-dependent manner, overview | Saccharomyces cerevisiae | orotate + 5-phospho-alpha-D-ribose 1-diphosphate | the compounds bind very tightly to the enzyme in a Mg2+-dependent manner, overview | ? |
Subunits | Comment | Organism |
---|---|---|
dimer | homodimer | Saccharomyces cerevisiae |
Synonyms | Comment | Organism |
---|---|---|
OPRTase | - |
Saccharomyces cerevisiae |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
assay at | Saccharomyces cerevisiae |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.8 | - |
assay at | Saccharomyces cerevisiae |