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 journalArticle

12 Citations (Scopus)

Abstract

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
Volume51
Issue number4
DOIs
Publication statusPublished - 2006

Keywords

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

Cite this

Xyn11A, a multidomain multicatalytic enzyme from Pseudobutyrivibrio xylanivorans Mz5(T). / Cepeljnik, Tadej; Rincon, Marco T.; Flint, Harry James; Marinsek-Logar, R.

In: Folia Microbiologica, Vol. 51, No. 4, 2006, p. 263-267.

Research output: Contribution to journalArticle

Cepeljnik, Tadej ; Rincon, Marco T. ; Flint, Harry James ; Marinsek-Logar, R. / Xyn11A, a multidomain multicatalytic enzyme from Pseudobutyrivibrio xylanivorans Mz5(T). In: Folia Microbiologica. 2006 ; Vol. 51, No. 4. pp. 263-267.
@article{1ba023d8972842869815e241b92f7f0f,
title = "Xyn11A, a multidomain multicatalytic enzyme from Pseudobutyrivibrio xylanivorans Mz5(T)",
abstract = "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.",
keywords = "cellulose binding domains, bacterium butyrivibrio fibrisolvens, xylanase genes xyna, Ruminococcus flavefaciens, Clostridium thermocellum, sequences, rumen, endoxylanases, expression, family 11",
author = "Tadej Cepeljnik and Rincon, {Marco T.} and Flint, {Harry James} and R. Marinsek-Logar",
year = "2006",
doi = "10.1007/BF02931809",
language = "English",
volume = "51",
pages = "263--267",
journal = "Folia Microbiologica",
issn = "0015-5632",
publisher = "Springer Netherlands",
number = "4",

}

TY - JOUR

T1 - Xyn11A, a multidomain multicatalytic enzyme from Pseudobutyrivibrio xylanivorans Mz5(T)

AU - Cepeljnik, Tadej

AU - Rincon, Marco T.

AU - Flint, Harry James

AU - Marinsek-Logar, R.

PY - 2006

Y1 - 2006

N2 - 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.

AB - 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.

KW - cellulose binding domains

KW - bacterium butyrivibrio fibrisolvens

KW - xylanase genes xyna

KW - Ruminococcus flavefaciens

KW - Clostridium thermocellum

KW - sequences

KW - rumen

KW - endoxylanases

KW - expression

KW - family 11

U2 - 10.1007/BF02931809

DO - 10.1007/BF02931809

M3 - Article

VL - 51

SP - 263

EP - 267

JO - Folia Microbiologica

JF - Folia Microbiologica

SN - 0015-5632

IS - 4

ER -