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柯萨奇病毒3C蛋白酶对肽底物的切割特异性

Cleavage specificity of coxsackievirus 3C proteinase for peptide substrate.

作者信息

Miyashita K, Okunishi J, Utsumi R, Komano T, Tamura T, Satoh N

机构信息

Central Research Laboratories, Maruishi Pharmaceutical Co., Ltd., Osaka, Japan.

出版信息

Biosci Biotechnol Biochem. 1996 Apr;60(4):705-7. doi: 10.1271/bbb.60.705.

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.

摘要

利用底物肽Ac-EALFQGPPV的C末端截短肽,在可裂解键的C末端侧研究了柯萨奇病毒3C蛋白酶(3Cpro)的底物需求。不仅Ac-EALFQG-NH2的Gln-Gly键,而且Ac-EALFQ-NH2的C末端酰胺基团都被3Cpro水解,这表明柯萨奇病毒3Cpro切割的必需残基存在于N末端的5个残基内。

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