Mutational Analysis of the Putative Substrate-binding Site of 3C Proteinase of Coxsackievirus B3
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概要
- 論文の詳細を見る
Single amino acid substitutions were introduced into the putative substrate-binding site of 3C proteinase (3C^<pro>) of coxsackievirus B3, a member of the picornavirus family. Mutations at either Thr142, His161, Gly164, Gly169, or Ala172 severely impaired or abolished the proteolytic activity except that a conservative Thr142to Ser mutant had detectable activity. These results, which have shown the participation of the 5 residues in 3C^<pro> activity, are consistent with the earlier predictions that these residues might be involved in substrate binding.
- 社団法人日本農芸化学会の論文
- 1995-01-23
著者
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Komano T
Kyoto Univ. Kyoto Jpn
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Komano Tohru
Laboratory Of Biochemistry Department Of Agricultural Chemistry Kyoto University
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Komano Tohru
京都大学
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MIYASHITA Kinji
Central Research Laboratories, Maruishi Pharmaceutical Co., Ltd.
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UTSUMI Ryutaro
Laboratory of Biochemistry, Department of Agricultural Chemistry, Kinki University
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SATOH Nobukatsu
Central Research Laboratories, Maruishi Pharmaceutical Co., Ltd.
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Utsumi R
Department Of Bioscience And Biotechnology Graduate School Of Agriculture Kinki University
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Satoh Nobukatsu
Central Research Laboratories Maruishi Pharmaceutical Co. Ltd.
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Utsumi Tomoyuki
Laboratory of Biochemistry, Department of Agricultural Chemistry, Kinki University
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Miyashita Kinji
Central Research Laboratories Maruishi Pharmaceutical Co. Ltd.
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Komano T
Laboratory Of Cellular Biochemistry Division Of Applied Life Sciences Graduate School Of Agriculture
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Utsumi Tomoyuki
Laboratory Of Biochemistry Department Of Agricultural Chemistry Kinki University
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