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 | Pyruvate oxidase |
Enzyme Information
| 1.2.3.3 |
Pyruvate oxidase.
based on mapping to UniProt P37063
Pyruvate + phosphate + O(2) = acetyl phosphate + CO(2) + H(2)O(2).
-!- Two reducing equivalents are transferred from the resonant carbanion/enamine forms of 2-hydroxyethyl-thiamine-diphosphate to the adjacent flavin cofactor, yielding 2-acetyl-thiamine diphosphate (AcThDP) and reduced flavin. -!- FADH is reoxidized by O(2) to yield H(2)O(2) and FAD and AcThDP is cleaved phosphorolytically to acetyl phosphate and thiamine diphosphate.
|
UniProtKB Entries (1)
| P37063 |
POXB_LACPL
Lactobacillus plantarum WCFS1
Pyruvate oxidase
|
PDB Structure
| PDB | 1Y9D |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
The role of Val-265 for Flavin Adenine Dinulceotide (FAD) binding in pyruvate oxidase: FTIR, kinetic and crystallographic studies on the enzyme variant V265A
Biochemistry
|