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

Date

Authors

Greene, Dina N

Whitney, Spencer

Matsumura, Ichiro

Publisher

Portland Press

Abstract

The 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 constraints

Keywords

Keywords: 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)

URI

http://hdl.handle.net/1885/49993

Collections

ANU Research Publications

Source

Biochemical Journal

Type

Journal article

DOI

10.1042/BJ20070071

Restricted until

2037-12-31

Downloads

File

Description

01_Greene_Artificially_evolved_2007.pdf (453.22 KB)