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

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dc.contributor.authorGreene, Dina N
dc.contributor.authorWhitney, Spencer
dc.contributor.authorMatsumura, Ichiro
dc.date.accessioned2015-12-10T22:13:55Z
dc.date.issued2007
dc.date.updated2015-12-09T08:01:22Z
dc.description.abstractThe 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
dc.identifier.issn0264-6021
dc.identifier.urihttp://hdl.handle.net/1885/49993
dc.publisherPortland Press
dc.sourceBiochemical Journal
dc.subjectKeywords: 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)
dc.titleArtificially evolved Synechococcus PCC6301 Rubisco variants exhibit improvements in folding and catalytic efficiency
dc.typeJournal article
local.bibliographicCitation.lastpage524
local.bibliographicCitation.startpage517
local.contributor.affiliationGreene, Dina N, Emory University
local.contributor.affiliationWhitney, Spencer, College of Medicine, Biology and Environment, ANU
local.contributor.affiliationMatsumura, Ichiro, Emory University
local.contributor.authoruidWhitney, Spencer, u9518388
local.description.embargo2037-12-31
local.description.notesImported from ARIES
local.identifier.absfor100104 - Genetically Modified Animals
local.identifier.absfor060107 - Enzymes
local.identifier.ariespublicationu9204316xPUB195
local.identifier.citationvolume404
local.identifier.doi10.1042/BJ20070071
local.identifier.scopusID2-s2.0-34250700987
local.type.statusPublished Version

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