ENZYME entry: EC 184.108.40.206
View entry in original ENZYME format
View entry in raw text format (no links)
|Pyranose dehydrogenase (acceptor).
|Quinone-dependent pyranose dehydrogenase.|
- 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
- A number of aldoses and ketoses in pyranose form, as well as
glycosides, gluco-oligosaccharides, sucrose and lactose can act as a
- 1,4-benzoquinone or ferricenium ion (ferrocene oxidized by removal of
one electron) can serve as acceptor.
- Unlike EC 220.127.116.11, this fungal enzyme does not interact with O(2)
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 18.104.22.168.
- Sugars are oxidized in their pyranose but not in their furanose form.
|PRIAM enzyme-specific profiles||22.214.171.124|
|KEGG Ligand Database for Enzyme Nomenclature||126.96.36.199|
|IUBMB Enzyme Nomenclature||188.8.131.52|
|MEDLINE||Find literature relating to 184.108.40.206|
|Rhea expert-curated reactions||220.127.116.11|
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.-.-.-