Due to scheduled maintenance work, this service will not be available from Tuesday August 23rd 06:00 pm until Wednesday August 24th 08:00 am CEST
. Apologies for the inconvenience.
ENZYME entry: EC 184.108.40.206
View entry in original ENZYME format
View entry in raw text format (no links)
|oligosaccharide reducing-end xylanase.
|reducing end xylose-releasing exo-oligoxylanase.|
|Hydrolysis of (1->4)-beta-D-xylose residues from the reducing end of oligosaccharides|
- The enzyme, originally isolated from the bacterium Bacillus
halodurans C-125, releases the xylose unit at the reducing end of
oligosaccharides ending with the structure beta-D-xylopyranosyl-
(1->4)-beta-D-xylopyranosyl-(1->4)-beta-D-xylopyranose, leaving the
new reducing end in the alpha configuration.
- It is specific for the beta anomers of xylooligosaccharides whose
degree of polymerization is equal to or greater than 3.
- The penultimate residue must be beta-D-xylopyranose, but replacing
either of the flanking residues with glucose merely slows the rate
|PRIAM enzyme-specific profiles||220.127.116.11|
|KEGG Ligand Database for Enzyme Nomenclature||18.104.22.168|
|IUBMB Enzyme Nomenclature||22.214.171.124|
|MEDLINE||Find literature relating to 126.96.36.199|
|Rhea expert-curated reactions||188.8.131.52|
entries corresponding to 3.2.1.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 3.2.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 3.-.-.-