放線菌由来のキトサナーゼの構造と機能

DOI Web Site 参考文献23件
  • 深溝 慶
    Laboratory of Biophysical Chemistry, Faculty of Agriculture, Kinki University
  • 本多 裕司
    Laboratory of Biophysical Chemistry, Faculty of Agriculture, Kinki University
  • BOUCHER Isabelle
    Departement de Biologie, Faculty des Sciences, Universite de Sherbrooke
  • BRZEZINSKI Ryszard
    Departement de Biologie, Faculty des Sciences, Universite de Sherbrooke

書誌事項

タイトル別名
  • Structure and Function of Chitosanase from Streptomyces sp. N174
  • ホウセンキン ユライ ノ キトサナーゼ ノ コウゾウ ト キノウ

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抄録

The reaction mechanism of chitosanase from Streptomyces sp. N174 was investigated by analysis of the products from substrate, 25-35% acetylated chitosan or glucosamine (G1cN) oligosaccharide, using the wild-type enzyme and its site-directed mutants. The chitosanase was found to hydrolyze G1cNAc-G1cN linkages as well as G1cN-G1cN linkages in the chitinous polysaccharide chain. When the chitosanase digestion of G1cN hexamer was followed by 1H-NMR spectroscopy, only α-form was produced in the early stage of the reaction, indicating that the chitosanase is an inverting enzyme. The chitosanase hydrolyzed G1cN hexamer in an endo-splitting manner, producing predominantly trimer, and dimer and tetramer in lesser amounts. From site-directed mutagenesis studies, G1u22 and Asp40 were found to be essential for catalysis, and Asp37 was found to play an important role in the stabilization of active site structure.

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