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Literature summary extracted from
- Concerted proton transfer mechanism of Clostridium thermocellum ribose-5-phosphate isomerase (2013), J. Phys. Chem. B, 117, 9354-9361.
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 5.3.1.6 | D-ribose 5-phosphate | Acetivibrio thermocellus | - |
D-ribulose 5-phosphate | - |
r |  |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 5.3.1.6 | Acetivibrio thermocellus | A3DIL8 | - |
- |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 5.3.1.6 | D-ribose 5-phosphate | - |
Acetivibrio thermocellus | D-ribulose 5-phosphate | - |
r | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 5.3.1.6 | RPI | - |
Acetivibrio thermocellus |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 5.3.1.6 | metabolism | the enzyme plays an essential role in the pentose phosphate pathway and the Calvin cycle of photosynthesis | Acetivibrio thermocellus |
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Release 2023.1 (January 2023)
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