ArticleArchaea (Vancouver, B.C.)2012
Acetate activation in Methanosaeta thermophila: characterization of the key enzymes pyrophosphatase and acetyl-CoA synthetase.
Article in Archaea (Vancouver, B.C.), 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
19 citing papers in PubMed, 44 citations in OpenAlex.
- Drivers of methane-cycling archaeal abundances, community structure, and catabolic pathways in continental margin sediments.Frontiers in microbiology · 2025Article
- Biohythane production via anaerobic digestion process: fundamentals, scale-up challenges, and techno-economic and environmental aspects.Environmental science and pollution research international · 2024Review
- Article
- Hydrogen-independent COISME communications · 2024Article
- Methane production bymBio · 2023Article
- Acetate and Acetyl-CoA Metabolism of ANME-2 Anaerobic Archaeal Methanotrophs.Applied and environmental microbiology · 2023Article
- Alleviating glucose repression and enhancing respiratory capacity to increase itaconic acid production.Synthetic and systems biotechnology · 2023Article
- Effects of phenyl acids on different degradation phases during thermophilic anaerobic digestion.Frontiers in microbiology · 2023Article
- Several ways one goal-methanogenesis from unconventional substrates.Applied microbiology and biotechnology · 2020Review
- Betaine Modulates Rumen Archaeal Community and Functioning during Heat and Osmotic Stress ConditionsArchaea (Vancouver, B.C.) · 2020Article
- Review
- Acetate Metabolism in Archaea: Characterization of an Acetate Transporter and of Enzymes Involved in Acetate Activation and Gluconeogenesis inFrontiers in microbiology · 2020Article
- Determination of Microbial Maintenance in Acetogenesis and Methanogenesis by Experimental and Modeling Techniques.Frontiers in microbiology · 2019Article
- Metabolism and Occurrence of Methanogenic and Sulfate-Reducing Syntrophic Acetate Oxidizing Communities in Haloalkaline Environments.Frontiers in microbiology · 2018Article
- Comparative Analysis of Methanogenic Communities in Different Laboratory-Scale Anaerobic Digesters.Archaea (Vancouver, B.C.) · 2016Article
- Acetate Metabolism in Anaerobes from the Domain Archaea.Life (Basel, Switzerland) · 2015Review
- Methanogenic burst in the end-Permian carbon cycle.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Characteristics, process parameters, and inner components of anaerobic bioreactors.BioMed research international · 2014Review
- Genetic resources for methane production from biomass described with the Gene Ontology.Frontiers in microbiology · 2014Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The thermophilic methanogen Methanosaeta thermophila uses acetate as sole substrate for methanogenesis. It was proposed that the acetate activation reaction that is needed to feed acetate into the methanogenic pathway requires the hydrolysis of two ATP, whereas the acetate activation reaction in Methanosarcina sp. is known to require only one ATP. As these organisms live at the thermodynamic limit that sustains life, the acetate activation reaction in Mt. thermophila seems too costly and was thus reevaluated. It was found that of the putative acetate activation enzymes one gene encoding an AMP-forming acetyl-CoA synthetase was highly expressed. The corresponding enzyme was purified and characterized in detail. It catalyzed the ATP-dependent formation of acetyl-CoA, AMP, and pyrophosphate (PP(i)) and was only moderately inhibited by PP(i). The breakdown of PP(i) was performed by a soluble pyrophosphatase. This enzyme was also purified and characterized. The pyrophosphatase hydrolyzed the major part of PP(i) (K(M) = 0.27 ± 0.05 mM) that was produced in the acetate activation reaction. Activity was not inhibited by nucleotides or PP(i). However, it cannot be excluded that other PP(i)-dependent enzymes take advantage of the remaining PP(i) and contribute to the energy balance of the cell.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.