ArticleThe Journal of biological chemistry2008
Reaction mechanism and structural model of ADP-forming Acetyl-CoA synthetase from the hyperthermophilic archaeon Pyrococcus furiosus: evidence for a second active site histidine residue.
Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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26 citing papers in PubMed, 42 citations in OpenAlex.
- Crystal structure of 3-hydroxypropionyl-CoA synthetase (ADP-forming) fromCurrent research in structural biology · 2026Article
- Crystal structure of the 4-hydroxybutyryl-CoA synthetase (ADP-forming) from nitrosopumilus maritimus.Communications biology · 2024Article
- Analysis of nearly 3000 archaeal genomes from terrestrial geothermal springs sheds light on interconnected biogeochemical processes.Nature communications · 2024Article
- Applying biochemical and structural characterization of hydroxycinnamate catabolic enzymes from soil metagenome for lignin valorization strategies.Applied microbiology and biotechnology · 2022Article
- Glucose Metabolism and Acetate Switch in Archaea: the Enzymes in Haloferax volcanii.Journal of bacteriology · 2021Article
- Second distinct conformation of the phosphohistidine loop in succinyl-CoA synthetase.Acta crystallographica. Section D, Structural biology · 2021Article
- Genomic and enzymatic evidence of acetogenesis by anaerobic methanotrophic archaea.Nature communications · 2020Article
- First Observation of an Acetate Switch in a Methanogenic Autotroph (Microbiology insights · 2020Article
- An alkaline active feruloyl-CoA synthetase from soil metagenome as a potential key enzyme for lignin valorization strategies.PloS one · 2019Article
- Acetyl Phosphate as a Primordial Energy Currency at the Origin of Life.Origins of life and evolution of the biosphere : the journal of the International Society for the Study of the Origin of Life · 2018Article
- Single-Cell Genomics Reveals a Diverse Metabolic Potential of UncultivatedFrontiers in microbiology · 2018Article
- The Physiology of Phagocytosis in the Context of Mitochondrial Origin.Microbiology and molecular biology reviews : MMBR · 2017Review
- Investigating the mechanism of ADP-forming acetyl-CoA synthetase from the protozoan parasite Entamoeba histolytica.FEBS letters · 2017Article
- Structure of NDP-forming Acetyl-CoA synthetase ACD1 reveals a large rearrangement for phosphoryl transfer.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Article
- Potential Role of Acetyl-CoA Synthetase (acs) and Malate Dehydrogenase (mae) in the Evolution of the Acetate Switch in Bacteria and Archaea.Scientific reports · 2015Article
- Acetate Metabolism in Anaerobes from the Domain Archaea.Life (Basel, Switzerland) · 2015Review
- The primary pathway for lactate oxidation in Desulfovibrio vulgaris.Frontiers in microbiology · 2015Article
- Biochemical and kinetic characterization of the recombinant ADP-forming acetyl coenzyme A synthetase from the amitochondriate protozoan Entamoeba histolytica.Eukaryotic cell · 2014Article
- Methanotrophic archaea possessing diverging methane-oxidizing and electron-transporting pathways.The ISME journal · 2014Article
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4 authors at 1 institution in 1 country.
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Abstract
In Archaea, acetate formation and ATP synthesis from acetyl-CoA is catalyzed by an unusual ADP-forming acetyl-CoA synthetase (ACD) (acetyl-CoA + ADP + P(i) acetate + ATP + HS-CoA) catalyzing the formation of acetate from acetyl-CoA and concomitant ATP synthesis by the mechanism of substrate level phosphorylation. ACD belongs to the protein superfamily of nucleoside diphosphate-forming acyl-CoA synthetases, which also include succinyl-CoA synthetases (SCSs). ACD differs from SCS in domain organization of subunits and in the presence of a second highly conserved histidine residue in the beta-subunit, which is absent in SCS. The influence of these differences on structure and reaction mechanism of ACD was studied with heterotetrameric ACD (alpha(2)beta(2)) from the hyperthermophilic archaeon Pyrococcus furiosus in comparison with heterotetrameric SCS. A structural model of P. furiosus ACD was constructed suggesting a novel spatial arrangement of the subunits different from SCS, however, maintaining a similar catalytic site. Furthermore, kinetic and molecular properties and enzyme phosphorylation as well as the ability to catalyze arsenolysis of acetyl-CoA were studied in wild type ACD and several mutant enzymes. The data indicate that the formation of enzyme-bound acetyl phosphate and enzyme phosphorylation at His-257alpha, respectively, proceed in analogy to SCS. In contrast to SCS, in ACD the phosphoryl group is transferred from the His-257alpha to ADP via transient phosphorylation of a second conserved histidine residue in the beta-subunit, His-71beta. It is proposed that ACD reaction follows a novel four-step mechanism including transient phosphorylation of two active site histidine residues:
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