A 3-Hydroxypropionate/4-Hydroxybutyrate Autotrophic Carbon Dioxide Assimilation Pathway in Archaea

@article{Berg2007A3A,
  title={A 3-Hydroxypropionate/4-Hydroxybutyrate Autotrophic Carbon Dioxide Assimilation Pathway in Archaea},
  author={I. Berg and Daniel Kockelkorn and W. Buckel and G. Fuchs},
  journal={Science},
  year={2007},
  volume={318},
  pages={1782 - 1786}
}
The assimilation of carbon dioxide (CO2) into organic material is quantitatively the most important biosynthetic process. We discovered that an autotrophic member of the archaeal order Sulfolobales, Metallosphaera sedula, fixed CO2 with acetyl–coenzyme A (acetyl-CoA)/propionyl-CoA carboxylase as the key carboxylating enzyme. In this system, one acetyl-CoA and two bicarbonate molecules were reductively converted via 3-hydroxypropionate to succinyl-CoA. This intermediate was reduced to 4… Expand
Conversion of 4-Hydroxybutyrate to Acetyl Coenzyme A and Its Anapleurosis in the Metallosphaera sedula 3-Hydroxypropionate/4-Hydroxybutyrate Carbon Fixation Pathway
TLDR
Transcriptomic analysis revealed the importance of the 3HP/4HB pathway in supplying acetyl-CoA to anabolic pathways generating intermediates in M. sedula metabolism, and provided the framework for examining connections between CO2 fixation and central metabolism in the sedula. Expand
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Ammonia-oxidizing archaea of the phylum Thaumarchaeota are among the most abundant organisms that exert primary control of oceanic and soil nitrification and are responsible for a large part of darkExpand
A dicarboxylate/4-hydroxybutyrate autotrophic carbon assimilation cycle in the hyperthermophilic Archaeum Ignicoccus hospitalis
TLDR
This work presents the complete metabolic cycle by which the primary CO2 acceptor molecule acetyl-CoA is regenerated, and combines anaerobic metabolic modules to a straightforward and efficient CO2 fixation mechanism. Expand
Role of 4-Hydroxybutyrate-CoA Synthetase in the CO2 Fixation Cycle in Thermoacidophilic Archaea*
TLDR
Transcriptomic analysis of cells grown under strict H2-CO2 autotrophy was consistent with the involvement of Msed_0406 and Msed-0394, and the identification of the 4-HB CoA synthetase now completes the set of enzymes comprising the 3HP/4HB cycle. Expand
3-Hydroxypropionyl-Coenzyme A Dehydratase and Acryloyl-Coenzyme A Reductase, Enzymes of the Autotrophic 3-Hydroxypropionate/4-Hydroxybutyrate Cycle in the Sulfolobales
TLDR
The findings indicate that the autotrophic carbon fixation cycles in Chloroflexus and in the Sulfolobales evolved independently and that different genes/enzymes have been recruited in the two lineages that catalyze the same kinds of reactions. Expand
Autotrophic Carbon Dioxide Assimilation in Thermoproteales Revisited
TLDR
It is concluded that the dicarboxylate/4-hydroxybutyrate cycle is operating in CO(2) fixation in the strict anaerobic Thermoproteales as well as in Desulfurococcales. Expand
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TLDR
A reaction kinetics model was developed to examine the biological and biotechnological attributes of the 3HP/4HB cycle as it operates in Metallosphaera sedula and assess metabolic engineering strategies for incorporating CO2 into chemical intermediates and products of bioteschnological importance: acetyl-CoA, succinate, and 3-hydroxypropionate. Expand
Enzymes Catalyzing Crotonyl-CoA Conversion to Acetoacetyl-CoA During the Autotrophic CO2 Fixation in Metallosphaera sedula
TLDR
It is shown that a model autotrophic member of Sulfolobales, Metallosphaera sedula, possesses in addition to the bifunctional protein (Msed_0399) several separate genes coding for crotonyl-CoA hydratase and (S)-3-hydroxybutyryl- CoA dehydrogenase, strengthening this conclusion. Expand
Labeling and Enzyme Studies of the Central Carbon Metabolism in Metallosphaera sedula
TLDR
The picture of the central carbon metabolism in autotrophic Sulfolobales is completed by connecting the autosphaera sedula carbon fixation cycle to the formation of central carbon precursor metabolites. Expand
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The data indicate that the reductive acetyl-CoA pathway is the only functioning CO(2) fixation pathway in 'A. Expand
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