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

Accepted Name
Oligosaccharide reducing-end xylanase.
Alternative Name(s)
Reducing end xylose-releasing exo-oligoxylanase.
Reaction catalysed
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 greatly.
PRIAM enzyme-specific profiles3.2.1.156
KEGG Ligand Database for Enzyme Nomenclature3.2.1.156
IUBMB Enzyme Nomenclature3.2.1.156
MEDLINEFind literature relating to

View entry in original ENZYME format
View entry in raw text format (no links)

All UniProtKB/Swiss-Prot entries referenced in this entry, with possibility to download in different formats, align etc.
All ENZYME / UniProtKB/Swiss-Prot 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.-.-.-