Mechanistic insights into the 1,3-xylanases: Useful enzymes for manipulation of algal biomass

Ethan D. Goddard-Borger, Keishi Sakaguchi, Stephan Reitinger, Nobuhisa Watanabe, Makoto Ito, Stephen G. Withers

Research output: Contribution to journalArticlepeer-review

18 Citations (Scopus)


Xylanases capable of degrading the crystalline microfibrils of 1,3-xylan that reinforce the cell walls of some red and siphonous green algae have not been well studied, yet they could prove to be of great utility in algaculture for the production of food and renewable chemical feedstocks. To gain a better mechanistic understanding of these enzymes, a suite of reagents was synthesized and evaluated as substrates and inhibitors of an endo-1,3-xylanase. With these reagents, a retaining mechanism was confirmed for the xylanase, its catalytic nucleophile identified, and the existence of -3 to +2 substrate-binding subsites demonstrated. Protein crystal X-ray diffraction methods provided a high resolution structure of a trapped covalent glycosyl-enzyme intermediate, indicating that the 1,3-xylanases likely utilize the 1S 34H 34C 1 conformational itinerary to effect catalysis.

Original languageEnglish
Pages (from-to)3895-3902
Number of pages8
JournalJournal of the American Chemical Society
Issue number8
Publication statusPublished - Feb 29 2012

All Science Journal Classification (ASJC) codes

  • Catalysis
  • General Chemistry
  • Biochemistry
  • Colloid and Surface Chemistry


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