Importance of five amino acid residues at C-terminal region for the folding and stability of β-glucosidase of Cellvibrio gilvus

To determine the role of the C-terminal region of Cellvibrio 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 ΔRGRAR, could be folded into an active form when expressed with...

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Published in:Journal of fermentation and bioengineering 1998-01, Vol.85 (4), p.433-435
Main Authors: Kim, Jong Deog, Singh, Satya, Machida, Sachiko, Yu, Young, Aoyagi, Chika, Kawata, Yasushi, Hayashi, Kiyoshi
Format: Article
Language:English
Subjects:
BACTERIA
BETA GLUCOSIDASA
BETA GLUCOSIDASE
Biological and medical sciences
Biotechnology
Cellvibrio gilvus
CHEMICAL STRUCTURE
deletion mutant
ESTRUCTURA QUIMICA
folding
formula omitted
Fundamental and applied biological sciences. Psychology
Methods. Procedures. Technologies
MUTANT
MUTANTES
MUTANTS
Protein engineering
STRUCTURE CHIMIQUE
β-glucosidase
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Summary:To determine the role of the C-terminal region of Cellvibrio 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 ΔRGRAR, could be folded into an active form when expressed 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.
ISSN:0922-338X
DOI:10.1016/S0922-338X(98)80089-5