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Related Experiment Video

Updated: Jun 3, 2026

Sequencing of Plant Wall Heteroxylans Using Enzymic, Chemical (Methylation) and Physical (Mass Spectrometry, Nuclear Magnetic Resonance) Techniques
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Sequencing of Plant Wall Heteroxylans Using Enzymic, Chemical (Methylation) and Physical (Mass Spectrometry, Nuclear Magnetic Resonance) Techniques

Published on: March 24, 2016

Structure and function of an arabinoxylan-specific xylanase.

Márcia A S Correia1, Koushik Mazumder, Joana L A Brás

  • 1Centro de Investigação Interdisciplinar em Sanidade Animal, Faculdade de Medicina Veterinária, Universidade Técnica de Lisboa, Avenida da Universidade Técnica, 1300-477 Lisboa, Portugal.

The Journal of Biological Chemistry
|March 8, 2011
PubMed
Summary

A novel enzyme, CtXyl5A from Clostridium thermocellum, specifically degrades decorated plant polysaccharides like arabinoxylans. Its unique structure reveals a pocket accommodating arabinofuranose, explaining its specificity for complex plant cell wall components.

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OLIgo Mass Profiling (OLIMP) of Extracellular Polysaccharides
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OLIgo Mass Profiling (OLIMP) of Extracellular Polysaccharides

Published on: June 20, 2010

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Last Updated: Jun 3, 2026

Sequencing of Plant Wall Heteroxylans Using Enzymic, Chemical (Methylation) and Physical (Mass Spectrometry, Nuclear Magnetic Resonance) Techniques
11:49

Sequencing of Plant Wall Heteroxylans Using Enzymic, Chemical (Methylation) and Physical (Mass Spectrometry, Nuclear Magnetic Resonance) Techniques

Published on: March 24, 2016

High-throughput Screening of Carbohydrate-degrading Enzymes Using Novel Insoluble Chromogenic Substrate Assay Kits
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OLIgo Mass Profiling (OLIMP) of Extracellular Polysaccharides
08:43

OLIgo Mass Profiling (OLIMP) of Extracellular Polysaccharides

Published on: June 20, 2010

Area of Science:

  • Biochemistry
  • Enzymology
  • Structural Biology

Background:

  • Plant cell wall degradation is crucial for the carbon cycle and has industrial relevance.
  • Xylanases degrade xylan but struggle with decorated polysaccharides like arabinoxylans.

Purpose of the Study:

  • To investigate the enzymatic activity and structure of CtXyl5A from Clostridium thermocellum.
  • To understand the molecular basis for CtXyl5A's specificity towards arabinoxylans.

Main Methods:

  • Enzyme activity assays on various xylan substrates.
  • Product analysis using chromatography.
  • X-ray crystallography of the catalytic module (CtGH5) and carbohydrate-binding module (CtCBM6).

Main Results:

  • CtXyl5A specifically hydrolyzes arabinoxylans, not unsubstituted xylans.
  • Oligosaccharide products consistently feature an O3 arabinose linked to the reducing end xylose.
  • Crystal structure reveals a pocket accommodating arabinofuranose, key for specificity.
  • CtCBM6 binds oligosaccharide termini.

Conclusions:

  • CtXyl5A possesses unique specificity for decorated xylans due to a dedicated arabinofuranose-binding pocket.
  • The enzyme's catalytic and binding modules interact via a hydrophobic interface, suggesting functional interdependence.