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

研究成果: Contribution to journalArticle査読

13 被引用数 (Scopus)

抄録

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.

本文言語英語
ページ(範囲)3895-3902
ページ数8
ジャーナルJournal of the American Chemical Society
134
8
DOI
出版ステータス出版済み - 2 29 2012

All Science Journal Classification (ASJC) codes

  • 触媒
  • 化学 (全般)
  • 生化学
  • コロイド化学および表面化学

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