Structural and functional analysis of glycosidases from plants that have a novel active center

2017 Fiscal Year Final Research Report

• Project/Area Number: 26660083
• Research Category: Grant-in-Aid for Challenging Exploratory Research
• Allocation Type: Multi-year Fund
• Research Field: Applied biochemistry
• Research Institution: The University of Tokyo
• Principal Investigator: Fushinobu Shinya 東京大学, 大学院農学生命科学研究科(農学部), 教授 (00302589)
• Research Collaborator: FUJITA Kiyotaka 鹿児島大学, 農学部, 准教授 ; ISHIWATA Akihiro 理化学研究所, 専任研究員 ; ITO Yukishige 理化学研究所, 主任研究員 ; Beckham Gregg T. 米国NREL, 研究員
• Project Period (FY): 2014-04-01 – 2018-03-31
• Keywords: グリコシダーゼ / シロイヌナズナ / イネ / β-アラビノオリゴ糖

Outline of Final Research Achievements

We initially aimed to study the structure and function of uncharacterized enzyme from plants that belong to DUF1680. Although we examined heterologous expression of the genes from Arabidopsis thaliana and Oryza sativa under various conditions, they did not express or expressed as insoluble aggregates. We determined a novel crystal structure of a GH146 β-L-arabinofuranosidase from plant pathogen, Xanthomonas. The active site of the Xanthomonas enzyme was cysteine, like the case of GH127 enzyme (HypBA1), and the enzyme had a novel carbohydrate-binding module domain.

Free Research Field

酵素学、構造生物学、農芸化学