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Literature summary for 2.2.1.1 extracted from
- New evidence for cofactors amino group function in thiamin catalysis by transketolase (2008), Biochem. Biophys. Res. Commun., 366, 692-697.
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Saccharomyces cerevisiae | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Saccharomyces cerevisiae |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 37 | - |
- |
Saccharomyces cerevisiae |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| beta-hydroxypyruvate + ? | - |
Saccharomyces cerevisiae | ? | - |
? |  |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| additional information | as opposed to the kinetically stabilized carbanion/enamine intermediate in transketolase when reconstituted with the native cofactor, 2-(1,2-dihydroxyethyl)-4'-monomethylaminothiamin diphosphate is rapidly released from the active centers during turnover and accumulates in the medium on a preparative scale | Saccharomyces cerevisiae |
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Release 2023.1 (January 2023)
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