Xyn11A, a multidomain multicatalytic enzyme from Pseudobutyrivibrio xylanivorans Mz5(T)

Tadej Cepeljnik, Marco T. Rincon, Harry James Flint, R. Marinsek-Logar

Research output: Contribution to journalArticlepeer-review

14 Citations (Scopus)


The rumen bacterium Pseudobutyrivibrio xylanivorans Mz5(T) has a potent xylanolytic enzyme system. A small native peptide (approximate to 30-kDa, designated Xyn11A) from the bacterium was first isolated and characterized by Edman degradation. The gene coding for Xyn11A was identified using PCR amplification with consensus primers. It was then fully sequenced to reveal an open reading frame of 1809 bp. The predicted N-terminal domain exhibited xylanolytic activity and was classed to the family I I of glycosyl hydrolases; it is followed by a region with homology to a family 6 cellulose binding module. The C-terminal domain codes for a putative NodB-like polysaccharide deacetylase which is predicted to be an acetyl esterase implicated in debranching activity in the xylan backbone. As similar domain organization was also found in several other xylanases from a diverse range of bacteria, a common ancestor of such a xylanase is considered to be present and spread, possibly by horizontal gene transfer, to other microorganisms from different ecological niches.

Original languageEnglish
Pages (from-to)263-267
Number of pages5
JournalFolia Microbiologica
Issue number4
Publication statusPublished - 2006


  • cellulose binding domains
  • bacterium butyrivibrio fibrisolvens
  • xylanase genes xyna
  • Ruminococcus flavefaciens
  • Clostridium thermocellum
  • sequences
  • rumen
  • endoxylanases
  • expression
  • family 11


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