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Improved Catalytic Activity of a Purified Multienzyme from a Modular Polyketide Synthase after Coexpression with Streptomyces Chaperonins in Escherichia coli .
Author(s) -
Betancor Lorena,
Fernández MaríaJosé,
Weissman Kira J.,
Leadlay Peter F.
Publication year - 2008
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.200800475
Subject(s) - polyketide , chaperonin , escherichia coli , groes , streptomyces , streptomyces coelicolor , polyketide synthase , biology , biochemistry , groel , bacteria , protein engineering , computational biology , protein folding , enzyme , gene , genetics , biosynthesis
Folding helpers : Coexpression of Streptomyces coelicolor chaperonins GroEL1, GroEL2 and GroES with an actinomycete‐derived polyketide synthase multienzyme in Escherichia coli has beneficial effects on yield, folding and specific activity of the purified enzyme. The results strongly suggest the utility of chaperones derived from polyketide‐producing actinomycete bacteria in optimising the recombinant production of PKS proteins in E. coli for detailed studies of structure and function.