Activating Compound | Comment | Organism | Structure |
---|---|---|---|
D-erythritol 4-phosphate | activates the decarboxylation of 5-fluoroorotate. This activation is due to the utilization of binding energy from interactions between OMPDC and activator | Saccharomyces cerevisiae | |
D-glycerol 3-phosphate | activates the decarboxylation of 5-fluoroorotate. | Saccharomyces cerevisiae | |
phosphite dianion | the activation with substrate 1-(beta-D-erythrofuranosyl)-orotate is due to the utilization of binding energy from interactions between OMPDC and activator to drive a complex conformational change from inactive open OMPDC (EO) to the active closed caged complex (EC), where EC is stabilized relative to EO by interactions between dianions and the side chains of Q215, Y217, and R235 | Saccharomyces cerevisiae |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | substrate specificity and kinetic analysis, overview | Saccharomyces cerevisiae |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
Orotidine 5'-phosphate | Saccharomyces cerevisiae | - |
UMP + CO2 | - |
? | |
Orotidine 5'-phosphate | Saccharomyces cerevisiae ATCC 204508 / S288c | - |
UMP + CO2 | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Saccharomyces cerevisiae | P03962 | - |
- |
Saccharomyces cerevisiae ATCC 204508 / S288c | P03962 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
1-(beta-D-erythrofuranosyl)-5-fluoroorotate | - |
Saccharomyces cerevisiae | 1-(beta-D-erythrofuranosyl)-5-fluorouracil + CO2 | - |
? | |
1-(beta-D-erythrofuranosyl)-5-fluoroorotate | - |
Saccharomyces cerevisiae ATCC 204508 / S288c | 1-(beta-D-erythrofuranosyl)-5-fluorouracil + CO2 | - |
? | |
1-(beta-D-erythrofuranosyl)-orotate | - |
Saccharomyces cerevisiae | 1-(beta-D-erythrofuranosyl)uracil + CO2 | - |
? | |
1-(beta-D-erythrofuranosyl)-orotate | - |
Saccharomyces cerevisiae ATCC 204508 / S288c | 1-(beta-D-erythrofuranosyl)uracil + CO2 | - |
? | |
5-fluoroorotate | - |
Saccharomyces cerevisiae | 5-fluorouracil + CO2 | - |
? | |
additional information | extraordinary specificity of OMPDC in binding the decarboxylation transition state with a higher affinity compared with the substrate orotidine 5'-phosphate. Substrate specificity and kinetic analysis, structure-function analysis, detailed overview | Saccharomyces cerevisiae | ? | - |
? | |
additional information | extraordinary specificity of OMPDC in binding the decarboxylation transition state with a higher affinity compared with the substrate orotidine 5'-phosphate. Substrate specificity and kinetic analysis, structure-function analysis, detailed overview | Saccharomyces cerevisiae ATCC 204508 / S288c | ? | - |
? | |
orotate | - |
Saccharomyces cerevisiae | uracil + CO2 | - |
? | |
Orotidine 5'-phosphate | - |
Saccharomyces cerevisiae | UMP + CO2 | - |
? | |
Orotidine 5'-phosphate | stepwise mechanism via a UMP carbanion intermediate, modeling of the transition state stabilization | Saccharomyces cerevisiae | UMP + CO2 | - |
? | |
Orotidine 5'-phosphate | - |
Saccharomyces cerevisiae ATCC 204508 / S288c | UMP + CO2 | - |
? | |
Orotidine 5'-phosphate | stepwise mechanism via a UMP carbanion intermediate, modeling of the transition state stabilization | Saccharomyces cerevisiae ATCC 204508 / S288c | UMP + CO2 | - |
? |
Synonyms | Comment | Organism |
---|---|---|
OMPDC | - |
Saccharomyces cerevisiae |
Orotidine 5'-monophosphate decarboxylase | - |
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 | - |
assay at | Saccharomyces cerevisiae |
General Information | Comment | Organism |
---|---|---|
additional information | substrate specificity and kinetic analysis, structure-function analysis, detailed overview | Saccharomyces cerevisiae |
kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.0000003 | - |
Orotate | pH 7.0, 25°C, wild-type enzyme | Saccharomyces cerevisiae | |
0.00002 | - |
1-(beta-D-erythrofuranosyl)-orotate | pH 7.0, 25°C, wild-type enzyme | Saccharomyces cerevisiae | |
0.0001 | - |
orotidine 5'-phosphate | pH 7.0, 25°C, wild-type enzyme | Saccharomyces cerevisiae | |
0.00014 | - |
5-Fluoroorotate | pH 7.0, 25°C, wild-type enzyme | Saccharomyces cerevisiae |