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2012 Fiscal Year Final Research Report

Structure-function relationship of endo-type enzymes involved in plant cell surface proteoglycans

Research Project

  • PDF
Project/Area Number 22580110
Research Category

Grant-in-Aid for Scientific Research (C)

Allocation TypeSingle-year Grants
Section一般
Research Field Applied biochemistry
Research InstitutionNational Agriculture and Food Research Organization

Principal Investigator

KANEKO Satoshi  独立行政法人農業・食品産業技術総合研究機構, 食品総合研究所・食品バイオテクノ ロジー研究領域, 主任研究員 (90343821)

Project Period (FY) 2010 – 2012
Keywords酵素利用学 / 糖質関連酵素
Research Abstract

An endo-.-1,6-galactanase which act on thickening agent arabinogalactan was obtained from Streptomyces avermitilis. The substrate specificity and the crystal structure of the recombinant enzyme were elucidated. To understand the detail mechanism of substrate specificity of the endo-.-1,6-galactanase, the other endo-.-1,6-galactanase which consist from distinctive amino acid sequence was cloned and crystal of the recombinant enzyme was obtained. However, quality of the crystal was not enough to solve structure so that the mechanism of substrate specificity of the endo-.-1,6-galactanase could not be elucidated.

  • Research Products

    (2 results)

All 2013

All Journal Article (2 results) (of which Peer Reviewed: 2 results)

  • [Journal Article] Characterization of a α-L-rhamnosidase from Streptomyces avermitilis2013

    • Author(s)
      Hitomi Ichinose, Zui Fujimoto, and Satoshi Kaneko
    • Journal Title

      Biosci. Biotechnol. Biochem

      Volume: 77 Pages: 213-216

    • Peer Reviewed
  • [Journal Article] The structure of a Streptomycesavermitilis α-L-rhamnosidase reveals a novel carbohydrate-binding module CBM67 within the six-domain arrangement2013

    • Author(s)
      Zui Fujimoto, Adam Jackson, Mari Michikawa, Tomoko Maehara, Mitsuru Momma, Bernard Henrissat, Harry J. Gilbert, and Satoshi Kaneko
    • Journal Title

      J. Biol. Chem

      Volume: 288 Pages: 12376-12385

    • Peer Reviewed

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Published: 2014-08-29  

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