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Literature summary for 4.1.1.98 extracted from
- The role of UbiX in Escherichia coli coenzyme Q biosynthesis (2007), Arch. Biochem. Biophys., 467, 144-153.
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 3-octaprenyl-4-hydroxybenzoate | - |
Escherichia coli | 2-octaprenylphenol + CO2 | - |
? |  |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| ubiX | - |
Escherichia coli |
General Information
| General Information | Comment | Organism |
|---|---|---|
| malfunction | the Escherichia coli ubiX null mutant accumulates 4-hydroxy-3-octaprenylbenzoic acid, a coenzyme Q8 precursor, and shows decreased UbiG O-methyltransferase activity | Escherichia coli |
| metabolism | the enzyme is involved in the decarboxylation step in coenzyme Q biosynthesis | Escherichia coli |
| physiological function | the enzyme is required for production of coenzyme Q8 and growth on succinate media | Escherichia coli |
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Release 2023.1 (January 2023)
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