Importance of Five Amino Acid Residues at C-Tarminal Region for the Folding and Stability of β-Glucosidase of Cellvibrio gilvus
スポンサーリンク
概要
- 論文の詳細を見る
To determine the role of the C-terminal region of Cellvivbrio gilvus β-glucosidase, a deletion mutant was constructed lacking five amino acid residues(RGRAR), three of which were arginine, from the C-terminal end. The mutant, designated ΔRGBAR, could be folded into an active form when experssed with the molecular chaperons GroEL/ES. In comparison with the native enzyme, the optimum pH of the mutant ΔRGRAR shifted to the acidic region and the pH stability to the neutral region, while its heat stability decreased. No significant difference in the kinetic parameter K_m was observed. It was concluded that the RGRAR residues located at the C-terminal end are quite important for the stability of the enzyme and protein folding.
- 社団法人日本生物工学会の論文
- 1998-04-25
著者
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KAWATA Yasushi
Faculty of Engineering, Tottori University
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Kim Jong
National Veterinary Research And Quarantine Service
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Hayashi Kiyoshi
National Food Research Institute Ministry Of Agriculture Forestry And Fisheries
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AOYAGI CHIKA
National Food Research Institute, Kannondai
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Yu Young
National Food Research Institute Kannondai
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Aoyagi Chika
National Food Research Institute Kannondai
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Kim Jong
National Food Research Institute Kannondai:(present Address)department Of Biological Engineering Yos
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SINGH SATYA
National Food Research Institute, Kannondai
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MACHIDA SACHIKO
National Food Research Institute, Kannondai
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Singh Satya
National Food Research Institute Kannondai
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Kawata Yasushi
Faculty Of Engineering Tottori University
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Hayashi Kiyoshi
National Food Research Institute
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Hayashi Kiyoshi
National Food Research Institute Kannondai
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Machida Sachiko
National Food Research Institute
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