Author's Organization:Central Research Laboratories, Maruishi Pharmaceutical Co., Ltd. Central Research Laboratories, Maruishi Pharmaceutical Co., Ltd. Laboratory of Biochemistry, Department of Agricultural Chemistry, Kinki University Laboratory of Biochemistry, Department of Agricultural Chemistry, Kyoto University Central Research Laboratories, Maruishi Pharmaceutical Co., Ltd. Central Research Laboratories, Maruishi Pharmaceutical Co., Ltd.
The substrate requirements of coxsackievirus 3C proteinase (3Cpro) were investigated on the C-terminal side of the scissile bond using C-terminal truncated peptides of the substrate peptide Ac-EALFQGPPV. Not only the Gln-Gly bond of Ac-EALFQG-NH2 but also the C-terminal amide group of Ac-EALFQ-NH2 was hydrolyzed by 3Cpro, suggesting that the essential residues for cleavage by coxsackievirus 3Cpro would exist within the N-terminal 5 residues.
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