Departmental Bulletin Paper 〈原著〉タンパク質NMR法を用いたライムギ種子Family GH19キチナーゼの基質結合部位に関する研究

岡崎, 蓉子  ,  新家, 粧子  ,  大沼, 貴之  ,  深溝, 慶

〈Synopsis〉Substrate-binding cleft of a family GH19 chitinase from rye seeds (RSC-c) was investigated by NMR spectroscopy, and the amino acid residue involved in the sugar residue binding was identified by site-directed mutagenesis. Mutation of Trp72 of RSC-c significantly reduced the binding affinity of the substrate, suggesting that the tryptophan residue is important for sugar residue binding not only at the mutation site but also in more extended region of the binding cleft.

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