To improve security and privacy, we are moving our web pages and services from HTTP to HTTPS.
To give users of web services time to transition to HTTPS, we will support separate HTTP and HTTPS services until the end of 2017.
From January 2018 most HTTP traffic will be automatically redirected to HTTPS. [more...] View this page in https
ENZYME entry: EC 188.8.131.52
View entry in original ENZYME format
View entry in raw text format (no links)
in this entry
|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 184.108.40.206, 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 220.127.116.11.
- Sugars are oxidized in their pyranose but not in their furanose form.
|PRIAM enzyme-specific profiles||18.104.22.168|
|KEGG Ligand Database for Enzyme Nomenclature||22.214.171.124|
|IUBMB Enzyme Nomenclature||126.96.36.199|
|MEDLINE||Find literature relating to 188.8.131.52|
, with possibility to download in different formats, align etc.
entries corresponding to 1.1.99.-
entries corresponding to 1.1.-.-
entries corresponding to 1.-.-.-