ArticleExtremophiles : life under extreme conditions2008
The 2-oxoacid dehydrogenase multienzyme complex of Haloferax volcanii.
Article in Extremophiles : life under extreme conditions, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed, 11 citations in OpenAlex.
- Open Issues for Protein Function Assignment inGenes · 2021Article
- Glucose Metabolism and Acetate Switch in Archaea: the Enzymes in Haloferax volcanii.Journal of bacteriology · 2021Article
- Functional genomic and advanced genetic studies reveal novel insights into the metabolism, regulation, and biology of Haloferax volcanii.Archaea (Vancouver, B.C.) · 2011Article
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3 authors at 2 institutions in 2 countries.
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Abstract
Those aerobic archaea whose genomes have been sequenced possess four adjacent genes that, by sequence comparisons with bacteria and eukarya, appear to encode the component enzymes of a 2-oxoacid dehydrogenase multienzyme complex. However, no catalytic activity of any such complex has ever been detected in the archaea. In Thermoplasma acidophilum, evidence has been presented that the heterologously expressed recombinant enzyme possesses activity with the branched chain 2-oxoacids and, to a lesser extent, with pyruvate. In the current paper, we demonstrate that in Haloferax volcanii the four genes are transcribed as an operon in vivo. However, no functional complex or individual enzyme, except for the dihydrolipoamide dehydrogenase component, could be detected in this halophile grown on a variety of carbon sources. Dihydrolipoamide dehydrogenase is present at low catalytic activities, the level of which is increased three to fourfold when Haloferax volcanii is grown on the branched-chain amino acids valine, leucine and isoleucine.
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