| Accepted Name |
|---|
| pyranose dehydrogenase (acceptor)
|
| Alternative Name(s) |
|---|
| PDH |
| pyranose dehydrogenase |
| pyranose-quinone oxidoreductase |
| quinone-dependent pyranose dehydrogenase |
| Reaction catalysed |
|---|
- pyranose + acceptor = pyranos-2-ulose + reduced acceptor
- pyranose + acceptor = pyranos-3-ulose + reduced acceptor
- pyranose + acceptor = pyranos-2,3-diulose + reduced acceptor
- a pyranoside + acceptor = a pyranosid-3-ulose + reduced acceptor
- a pyranoside + acceptor = a pyranosid-3,4-diulose + reduced acceptor
|
| Comment(s) |
|---|
- A number of aldoses and ketoses in pyranose form, as well as
glycosides, gluco-oligosaccharides, sucrose and lactose can act as a
donor.
- 1,4-Benzoquinone or ferricenium ion (ferrocene oxidized by removal of
one electron) can serve as acceptor.
- Unlike EC 1.1.3.10, this fungal enzyme does not interact with O2 and
exhibits extremely broad substrate tolerance with variable
regioselectivity (C-3, C-2 or C-3 + C-2 or C-3 + C-4) for
(di)oxidation of different sugars.
- D-glucose is exclusively or preferentially oxidized at C-3 (depending
on the enzyme source), but can also be oxidized at C-2 + C-3.
- The enzyme also acts on 1->4-alpha- and 1->4-beta-gluco-
oligosaccharides, non-reducing gluco-oligosaccharides and
L-arabinose, which are not substrates of EC 1.1.3.10.
- Sugars are oxidized in their pyranose but not in their furanose form.
|
| Cross-references |
|---|
| BRENDA | 1.1.99.29 |
| EC2PDB | 1.1.99.29 |
| ExplorEnz | 1.1.99.29 |
| PRIAM enzyme-specific profiles | 1.1.99.29 |
| KEGG Ligand Database for Enzyme Nomenclature | 1.1.99.29 |
| IUBMB Enzyme Nomenclature | 1.1.99.29 |
| IntEnz | 1.1.99.29 |
| MEDLINE | Find literature relating to 1.1.99.29 |
| MetaCyc | 1.1.99.29 |
| Rhea expert-curated reactions | 1.1.99.29 |
| UniProtKB/Swiss-Prot |
|
View entry in original ENZYME format
View entry in raw text format (no links)
All
ENZYME /
UniProtKB/Swiss-Prot entries corresponding to 1.1.99.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.1.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.-.-.-
