EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.1.1.333 | Mycobacterium tuberculosis | P9WGS9 | Dpre2 | - |
1.1.1.333 | Mycobacterium tuberculosis H37Rv | P9WGS9 | Dpre2 | - |
1.1.98.3 | Mycobacterium tuberculosis | P9WJF1 | Dpre1 | - |
1.1.98.3 | Mycobacterium tuberculosis H37Rv | P9WJF1 | Dpre1 | - |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.1.1.333 | additional information | decaprenylphospho-beta-D-ribofuranose 2-oxidase DprE1 and decaprenylphospho-beta-D-erythro-pentofuranosid-2-ulose 2-reductase DprE2 together catalyze the epimerization of decaprenylphosphoryl-beta-D-ribofuranose to decaprenylphosphoryl-beta-D-arabinofuranose. Neither protein individually is sufficient to support the activity | Mycobacterium tuberculosis | ? | - |
? | |
1.1.1.333 | additional information | decaprenylphospho-beta-D-ribofuranose 2-oxidase DprE1 and decaprenylphospho-beta-D-erythro-pentofuranosid-2-ulose 2-reductase DprE2 together catalyze the epimerization of decaprenylphosphoryl-beta-D-ribofuranose to decaprenylphosphoryl-beta-D-arabinofuranose. Neither protein individually is sufficient to support the activity | Mycobacterium tuberculosis H37Rv | ? | - |
? | |
1.1.98.3 | additional information | decaprenylphospho-beta-D-ribofuranose 2-oxidase DprE1 and decaprenylphospho-beta-D-erythro-pentofuranosid-2-ulose 2-reductase DprE2 together catalyze the epimerization of decaprenylphosphoryl-beta-D-ribofuranose to decaprenylphosphoryl-beta-D-arabinofuranose. Neither protein individually is sufficient to support the activity | Mycobacterium tuberculosis | ? | - |
? | |
1.1.98.3 | additional information | decaprenylphospho-beta-D-ribofuranose 2-oxidase DprE1 and decaprenylphospho-beta-D-erythro-pentofuranosid-2-ulose 2-reductase DprE2 together catalyze the epimerization of decaprenylphosphoryl-beta-D-ribofuranose to decaprenylphosphoryl-beta-D-arabinofuranose. Neither protein individually is sufficient to support the activity | Mycobacterium tuberculosis H37Rv | ? | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.1.1.333 | Rv3791 | - |
Mycobacterium tuberculosis |
1.1.98.3 | Rv3790 | - |
Mycobacterium tuberculosis |
EC Number | General Information | Comment | Organism |
---|---|---|---|
1.1.1.333 | physiological function | decaprenylphosphoryl-D-arabinofuranose is synthesized by the following sequence of events: 5-phosphoribose 1-diphosphate is transferred to a decaprenyl-phosphate molecule to form decaprenylphosphoryl-beta-D-5-phosphoribose. Decaprenylphosphoryl-beta-D-5-phosphoribose is dephosphorylated to form decaprenylphosphoryl-beta-D-ribose. The hydroxyl group at the 2 position of the ribose is oxidized and is likely to form decaprenylphosphoryl-2-keto-beta-D-erythro-pentofuranose. Decaprenylphosphoryl-2-keto-beta-D-erythro-pentofuranose is reduced to form decaprenylphosphoryl-beta-D-arabinofuranose. Thus, the epimerization of the ribosyl to an arabinosyl residue occurs at the lipid-linked level | Mycobacterium tuberculosis |
1.1.98.3 | physiological function | decaprenylphosphoryl-D-arabinofuranose is synthesized by the following sequence of events: 5-phosphoribose 1-diphosphate is transferred to a decaprenyl-phosphate molecule to form decaprenylphosphoryl-beta-D-5-phosphoribose. Decaprenylphosphoryl-beta-D-5-phosphoribose is dephosphorylated to form decaprenylphosphoryl-beta-D-ribose. The hydroxyl group at the 2 position of the ribose is oxidized and is likely to form decaprenylphosphoryl-2-keto-beta-D-erythro-pentofuranose. Decaprenylphosphoryl-2-keto-beta-D-erythro-pentofuranose is reduced to form decaprenylphosphoryl-beta-D-arabinofuranose. Thus, the epimerization of the ribosyl to an arabinosyl residue occurs at the lipid-linked level | Mycobacterium tuberculosis |