Abstract
The rumen bacteriumPseudobutyrivibrio xylanivorans Mz5T has a potent xylanolytic enzyme system. A small native peptide (≈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 11 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.
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The first author was supported by aMarie Curie Fellowship Program andFEBS short-term fellowship program.
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Čepeljnik, T., Rincón, M.T., Flint, H.J. et al. Xyn11A, a multidomain multicatalytic enzyme fromPseudobutyrivibrio xylanivorans Mz5T . Folia Microbiol 51, 263–267 (2006). https://doi.org/10.1007/BF02931809
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DOI: https://doi.org/10.1007/BF02931809