〈Original 〉NMR study on the substrate-binding site of a family GH19 chitinase from rye seeds
岡崎, 蓉子 ,
新家, 粧子 ,
大沼, 貴之深溝, 慶
近畿大学農学部紀要 = MEMOIRS OF THE FACULTY OF AGRICULTURE OF KINKI UNIVERSITY
36 , 2016-03-31 , 近畿大学農学部
〈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.