CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.40 | 3-Layer(aba) Sandwich |
|
3.40.50 | Rossmann fold |
|
3.40.50.970 | Thiamin diphosphate (ThDP)-binding fold, Pyr/PP domains |
Domain Context
CATH Clusters
| Superfamily | 3.40.50.970 |
| Functional Family | Transketolase |
Enzyme Information
| 2.2.1.1 |
Transketolase.
based on mapping to UniProt P27302
Sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = D-ribose 5-phosphate + D-xylulose 5-phosphate.
-!- Wide specificity for both reactants, e.g. converts hydroxypyruvate and R-CHO into CO(2) and R-CHOH-CO-CH(2)OH. -!- The enzyme from the bacterium Alcaligenes faecalis shows high activity with D-erythrose 4-phosphate as acceptor.
|
UniProtKB Entries (1)
| P27302 |
TKT1_ECOLI
Escherichia coli K-12
Transketolase 1
|
PDB Structure
| PDB | 2R8P |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Strain and near attack conformers in enzymic thiamin catalysis: X-ray crystallographic snapshots of bacterial transketolase in covalent complex with donor ketoses xylulose 5-phosphate and fructose 6-phosphate, and in noncovalent complex with acceptor aldose ribose 5-phosphate.
Biochemistry
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