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ENZYME entry: EC 3.2.1.156

Accepted Name
Oligosaccharide reducing-end xylanase.
Alternative Name(s)
Reducing end xylose-releasing exo-oligoxylanase.
Rex.
Reaction catalysed
Hydrolysis of (1->4)-beta-D-xylose residues from the reducing end of oligosaccharides
Comment(s)
  • 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.
Cross-references
BRENDA3.2.1.156
EC2PDB3.2.1.156
ExplorEnz3.2.1.156
PRIAM enzyme-specific profiles3.2.1.156
KEGG Ligand Database for Enzyme Nomenclature3.2.1.156
IUBMB Enzyme Nomenclature3.2.1.156
IntEnz3.2.1.156
MEDLINEFind literature relating to 3.2.1.156
MetaCyc3.2.1.156
UniProtKB/Swiss-Prot
Q9KB30, REOX_BACHD;  A1A048, REOX_BIFAA;  

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All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 3.2.1.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 3.2.-.-
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