Artificially evolved Synechococcus PCC6301 Rubisco variants exhibit improvements in folding and catalytic efficiency

Greene, Dina NWhitney, SpencerMatsumura, Ichiro2015-12-100264-6021http://hdl.handle.net/1885/49993The photosynthetic CO2-fixing enzyme, Rubisco (ribulose-1,5-bisphosphate carboxylase/oxygenase), is responsible for most of the world's biomass, but is a slow non-specific catalyst. We seek to identify and overcome the chemical and biological constraintsKeywords: Amino acids; Biomass; Catalyst activity; Escherichia coli; Gene transfer; Mutagenesis; Photosynthesis; Directed evolution; Metabolic engineering; Protein engineering; Enzyme kinetics; chaperonin; dihydrolipoamide dehydrogenase; enzyme variant; messenger R CO 2 fixation; Directed evolution; Metabolic engineering; Protein engineering; Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco)Artificially evolved Synechococcus PCC6301 Rubisco variants exhibit improvements in folding and catalytic efficiency200710.1042/BJ200700712015-12-09