2018
DOI: 10.1016/j.copbio.2017.07.017
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A short history of RubisCO: the rise and fall (?) of Nature's predominant CO2 fixing enzyme

Abstract: Ribulose-1,5-bisphosphate carboxylase/oxygenase (RubisCO) is arguably one of the most abundant proteins in the biosphere and a key enzyme in the global carbon cycle. Although RubisCO has been intensively studied, its evolutionary origins and rise as Nature's most dominant carbon dioxide (CO)-fixing enzyme still remain in the dark. In this review we will bring together biochemical, structural, physiological, microbiological, as well as phylogenetic data to speculate on the evolutionary roots of the CO-fixation … Show more

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Cited by 254 publications
(203 citation statements)
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“…Rather, form III Rubiscos have a catabolic role in the removal of intermediates formed by ribonucleoside 5=-monophosphate catabolism and directing the ribose moiety carbons to central metabolism. The biochemical, structural, and phylogenetic relations of the Rubiscos have been reviewed in detail previously (104)(105)(106)(107)(108)(109).…”
Section: Rubiscomentioning
confidence: 99%
See 1 more Smart Citation
“…Rather, form III Rubiscos have a catabolic role in the removal of intermediates formed by ribonucleoside 5=-monophosphate catabolism and directing the ribose moiety carbons to central metabolism. The biochemical, structural, and phylogenetic relations of the Rubiscos have been reviewed in detail previously (104)(105)(106)(107)(108)(109).…”
Section: Rubiscomentioning
confidence: 99%
“…Form IV Rubisco catalyzing enolization without subsequent carboxylation may represent an ancestral Rubisco to which the carboxylation process was added later in evolution and where forms III, II/III, and I appeared. Additionally, the Calvin-Benson-Bassham cycle may have evolved from ancient nucleotide metabolism (108). In line with this suggestion, Schönheit and colleagues proposed that "a simple interpretation is that the type III Rubisco pathway [i.e., the pentose bisphosphate pathway] is an ancient relic of the first heterotrophic metabolisms in archaea, Rubisco later being transferred to bacteria, where it is less common among obligate heterotrophs, and, where it-in timeultimately became assimilated into dedicated carbon dioxide fixation in the Calvin[-Benson-Bassham] cycle" and that "ribose was probably the first abundant sugar" (157), and as mentioned above, PRibP may be regarded as an ancient phosphoribosyl donor that became replaced by PRPP in "modern" organisms.…”
Section: Evolution and Phylogenymentioning
confidence: 99%
“…Besides the reductive acetyl-CoA pathway and the reductive TCA cycleboth of which are believed to have originated early in the evolution of metabolism 10 the other carbon fixation routes are thought to have evolved by recruiting enzymes from other metabolic pathways. For example, Rubiscothe carboxylating enzyme of the RuBP cycleprobably evolved from a non-CO2-fixing ancestral enzyme, thus emerging in a non-autotrophic context 11 . Similarly, acetyl-CoA carboxylase likely originated as a key component of fatty acid biosynthesis before being recruited into carbon fixation pathways in several prokaryotic lineages 2,3 .…”
Section: Introductionmentioning
confidence: 99%
“…The Calvin-Benson-Bassham (CBB) cycle 1 is the predominant of the six naturally occurring CO 2 fixation pathways 2,3 . Its key enzyme ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO) is considered to be the most abundant enzyme found in the biosphere and fixates around 90% of the inorganic carbon converted into biomass 4 .…”
Section: Introductionmentioning
confidence: 99%