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Co‐refolding of two peptide fragments derived from Agrobacterium tumefaciens β‐glucosidase with catalytic activity
Author(s) -
Kim Bong-Jo,
Mangala Selanere L.,
Hayashi Kiyoshi
Publication year - 2005
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2005.04.065
Subject(s) - agrobacterium tumefaciens , amino acid , enzyme , biochemistry , chemistry , peptide , n terminus , c terminus , peptide sequence , gene , stereochemistry , transformation (genetics)
Four sites of the non‐homologous region (coding amino acid residues of 347, 421, 466 and 533) of a gene were randomly selected for splitting to investigate the function of β‐glucosidase from Agrobacterium tumefaciens in the co‐refolding of peptides into the catalytically active enzyme. As a result of gene splitting, four N‐ and C‐terminal domain peptides were obtained as insoluble inclusion bodies. No catalytic activity was observed when these fragments refolded individually. However, a considerable amount of activity was restored when the two fragments derived from N‐ and C‐ terminal peptides were co‐refolded together. The deletion of amino acid residues in the non‐homologous region resulted in a complete loss of enzyme activity, which suggests that truncation of amino acids in this region strongly affects the co‐refolding ability of the enzyme to maintain activity.