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Literature summary for 4.1.1.23 extracted from
- Catalytic proficiency: the unusual case of OMP decarboxylase (2002), Annu. Rev. Biochem., 71, 847-885.
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| in complex with different ligands, e.g. 6-hydroxyuridine 5'-phosphate | Saccharomyces cerevisiae |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| D91A | mutant with strongly reduced activity, incapable of binding substrate | Saccharomyces cerevisiae |
| D96A | active site mutant with increased dissociation constants for various ligands and strongly reduced activity | Saccharomyces cerevisiae |
| K59A | active site mutant with increased dissociation constants for various ligands and strongly reduced activity | Saccharomyces cerevisiae |
| K93A | mutant with strongly reduced activity, incapable of binding substrate | Saccharomyces cerevisiae |
| R235A | active site mutant with increased dissociation constants for various ligands | Saccharomyces cerevisiae |
| Y217A | active site mutant with increased dissociation constants for various ligands | Saccharomyces cerevisiae |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| 5,6-dihydroorotidine 5'-phosphate | - |
Saccharomyces cerevisiae |  |
| 5-phosphoribofuranosylallopurinol | - |
Saccharomyces cerevisiae | |
| 6-azauridine 5'-phosphate | competitive inhibitor | Saccharomyces cerevisiae | |
| 6-carboxyamidouridine 5'-phosphate | - |
Saccharomyces cerevisiae | |
| 6-hydroxyuridine 5'-phosphate | potent competitive inhibitor | Saccharomyces cerevisiae | |
| 6-thiocarboxamidouridine 5'-phosphate | - |
Saccharomyces cerevisiae | |
| additional information | not inhibited by 2-thioorotidine 5'-phosphate | Saccharomyces cerevisiae | |
| Orotate | - |
Saccharomyces cerevisiae | |
| phosphate | - |
Saccharomyces cerevisiae | |
| ribose 5-phosphate | competitive inhibitor | Saccharomyces cerevisiae | |
| UMP | - |
Saccharomyces cerevisiae | |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | kinetic properties, catalytic proficiency/efficiency | Saccharomyces cerevisiae | |
| 0.0007 | - |
orotidine 5'-phosphate | - |
Saccharomyces cerevisiae | |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| additional information | no metal ion requirement | Saccharomyces cerevisiae |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| Orotidine 5'-phosphate | Bacillus subtilis | - |
UMP + CO2 | - |
? | |
| Orotidine 5'-phosphate | Escherichia coli | - |
UMP + CO2 | - |
? | |
| Orotidine 5'-phosphate | Saccharomyces cerevisiae | - |
UMP + CO2 | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bacillus subtilis | - |
- |
- |
| Escherichia coli | - |
- |
- |
| Saccharomyces cerevisiae | - |
- |
- |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| orotidine 5'-phosphate = UMP + CO2 | mechanism | Bacillus subtilis | |
| orotidine 5'-phosphate = UMP + CO2 | mechanism | Escherichia coli | |
| orotidine 5'-phosphate = UMP + CO2 | mechanism | Saccharomyces cerevisiae |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | 2-thioorotidine 5'-phosphate is 10000000fold less reactive than orotidine 5'-phosphate as substrate, not: 2-thiouridine 5'-phosphate | Saccharomyces cerevisiae | ? | - |
? | |
| Orotidine 5'-phosphate | - |
Bacillus subtilis | UMP + CO2 | - |
? | |
| Orotidine 5'-phosphate | - |
Escherichia coli | UMP + CO2 | - |
? | |
| Orotidine 5'-phosphate | - |
Saccharomyces cerevisiae | UMP + CO2 | - |
? | |
| Orotidine 5'-phosphate | catalytic proficiency, activity does not depend on the formation of a covalent bond to the substrate, catalyzes the reaction through noncovalent binding interactions that involve only the functional groups of its constituent amino acids, catalytic mechanism, mechanism of transition state stabilization, active site structure, role of Lys-93 | Saccharomyces cerevisiae | UMP + CO2 | - |
ir | |
| Orotidine 5'-phosphate | mechanism, enzyme structure | Bacillus subtilis | UMP + CO2 | - |
? | |
| Orotidine 5'-phosphate | mechanism, enzyme structure | Escherichia coli | UMP + CO2 | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| homodimer | active form, two independently operating active sites per dimer, located at the interface between subunits | Saccharomyces cerevisiae |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | - |
Saccharomyces cerevisiae |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 6.9 | - |
- |
Saccharomyces cerevisiae |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| additional information | no cofactor requirement | Saccharomyces cerevisiae |
Ki Value [mM]
| Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.0000000088 | - |
6-hydroxyuridine 5'-phosphate | - |
Saccharomyces cerevisiae | |
| 0.000064 | - |
6-azauridine 5'-phosphate | - |
Saccharomyces cerevisiae | |
| 0.08 | - |
ribose 5-phosphate | - |
Saccharomyces cerevisiae | |
| 0.2 | - |
UMP | - |
Saccharomyces cerevisiae | |
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