title: Cleavage specificity of coxsackievirus 3C proteinase for peptide substrate.
abstract: 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.
authors.affiliation: Central Research Laboratories, Maruishi Pharmaceutical Co., Ltd., Osaka, Japan.
authors.forename: K
authors.initials: K
authors.lastname: Miyashita
authors.forename: J
authors.initials: J
authors.lastname: Okunishi
authors.forename: R
authors.initials: R
authors.lastname: Utsumi
authors.forename: T
authors.initials: T
authors.lastname: Komano
authors.forename: T
authors.initials: T
authors.lastname: Tamura
authors.forename: N
authors.initials: N
authors.lastname: Satoh
mesh_terms: D000595:Amino Acid Sequence; D010450:Endopeptidases / Q000378:metabolism*; D004770:Enterovirus / Q000201:enzymology*; D008969:Molecular Sequence Data; D010455:Peptides / Q000378:metabolism*; D013379:Substrate Specificity
chemical_list: D010455:Peptides; D010450:Endopeptidases