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Literature summary for 2.4.2.10 extracted from
- Isolation and characterization of the orotidine 5'-monophosphate decarboxylase domain of the multifunctional protein uridine 5'-monophosphate synthase (1985), J. Biol. Chem., 260, 9443-9451.
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 51500 | - |
x * 51500, SDS-PAGE, sedimentation studies reveal monomer or dimer, enzyme activity and orotidine 5-monophosphate decarboxylating activity on a single polypeptide | Mus musculus |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Mus musculus | - |
- |
- |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| Ehrlich ascites carcinoma cell | - |
Mus musculus | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | enzyme from mammals is a bifunctional polypeptide, it also catalyzes the reaction listed as EC 4.1.1.23 | Mus musculus | ? | - |
? |  |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 51500, SDS-PAGE, sedimentation studies reveal monomer or dimer, enzyme activity and orotidine 5'-monophosphate decarboxylating activity on a single polypeptide | Mus musculus |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| More | enzyme from mammals is a bifunctional polypeptide, it also catalyzes the reaction listed as EC 4.1.1.23 | Mus musculus |
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Release 2023.1 (January 2023)
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