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Information on EC 3.2.1.156 - oligosaccharide reducing-end xylanase and Organism(s) Alkalihalobacillus halodurans and UniProt Accession Q9KB30

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IUBMB Comments
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.
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Alkalihalobacillus halodurans
UNIPROT: Q9KB30
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Word Map
The enzyme appears in selected viruses and cellular organisms
Synonyms
rex8a, reducing-end xylose-releasing exo-oligoxylanase, rxyn8, phxyl, reducing end xylose-releasing exo-oligoxylanase, oligosaccharide reducing-end xylanase, gh8 xylanase, more
SYSTEMATIC NAME
IUBMB Comments
beta-D-xylopyranosyl-(1->4)-beta-D-xylopyranose reducing-end xylanase
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.
CAS REGISTRY NUMBER
COMMENTARY hide
55126-95-9
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879497-03-7
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