About: Pyruvate synthase is a research topic. Over the lifetime, 181 publications have been published within this topic receiving 9506 citations. The topic is also known as: pyruvate:ferredoxin 2-oxidoreductase (CoA-acetylating) & pyruvate oxidoreductase.
TL;DR: Homogenates of Tritrichomonas foetus have pyruvate synthase and hydrogenase, but lack pyruVate-formate lyase and formate dehydrogenase, and these activities are in a subcellular particle identified previously as the site of malate and α-glycerophosphate dehydrogensases.
TL;DR: The biochemistry of acetogenesis is reviewed and the microbes that catalyze the reactions that are central to acetogenesis are described and the focus is on the enzymology of the process.
Abstract: The biochemistry of acetogenesis is reviewed. The microbes that catalyze the reactions that are central to acetogenesis are described and the focus is on the enzymology of the process. These microbes play a key role in the global carbon cycle, producing over 10 trillion kilograms of acetic acid annually. Acetogens have the ability to anaerobically convert carbon dioxide and CO into acetyl-CoA by the Wood-Ljungdahl pathway, which is linked to energy conservation. They also can convert the six carbons of glucose stoichiometrically into 3 mol of acetate using this pathway. Acetogens and other anaerobic microbes (e.g., sulfate reducers and methanogens) use the Wood-Ljungdahl pathway for cell carbon synthesis. Important enzymes in this pathway that are covered in this review are pyruvate ferredoxin oxidoreductase, CO dehydrogenase/acetyl-CoA synthase, a corrinoid iron-sulfur protein, a methyltransferase, and the enzymes involved in the conversion of carbon dioxide to methyl-tetrahydrofolate.
TL;DR: 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.
Abstract: Ignicoccus hospitalis is an anaerobic, autotrophic, hyperthermophilic Archaeum that serves as a host for the symbiotic/parasitic Archaeum Nanoarchaeum equitans It uses a yet unsolved autotrophic CO(2) fixation pathway that starts from acetyl-CoA (CoA), which is reductively carboxylated to pyruvate Pyruvate is converted to phosphoenol-pyruvate (PEP), from which glucogenesis as well as oxaloacetate formation branch off Here, we present the complete metabolic cycle by which the primary CO(2) acceptor molecule acetyl-CoA is regenerated Oxaloacetate is reduced to succinyl-CoA by an incomplete reductive citric acid cycle lacking 2-oxoglutarate dehydrogenase or synthase Succinyl-CoA is reduced to 4-hydroxybutyrate, which is then activated to the CoA thioester By using the radical enzyme 4-hydroxybutyryl-CoA dehydratase, 4-hydroxybutyryl-CoA is dehydrated to crotonyl-CoA Finally, beta-oxidation of crotonyl-CoA leads to two molecules of acetyl-CoA Thus, the cyclic pathway forms an extra molecule of acetyl-CoA, with pyruvate synthase and PEP carboxylase as the carboxylating enzymes The proposal is based on in vitro transformation of 4-hydroxybutyrate, detection of all enzyme activities, and in vivo-labeling experiments using [1-(14)C]4-hydroxybutyrate, [1,4-(13)C(2)], [U-(13)C(4)]succinate, or [1-(13)C]pyruvate as tracers The pathway is termed the dicarboxylate/4-hydroxybutyrate cycle It combines anaerobic metabolic modules to a straightforward and efficient CO(2) fixation mechanism
TL;DR: The results described here demonstrate that the Clostridium thermoaceticum PFOR is a highly efficient pyruvate synthase in vivo andMeasurements of itsk cat/K m values demonstrate that ferredoxin is ahighly efficient electron carrier in both the oxidative and reductive reactions.
TL;DR: The enzyme that catalyzes the terminal oxidation step, pyruvate ferredoxin oxidoreductase (POR), has now been purified and it is proposed that P. furiosus POR may represent an ancestral form of a pyruVate-oxidizing enzyme.