pyruvate synthase | |||||||||
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Identifiers | |||||||||
EC no. | 1.2.7.1 | ||||||||
CAS no. | 9082-51-3 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
Gene Ontology | AmiGO / QuickGO | ||||||||
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In enzymology, a pyruvate synthase (EC 1.2.7.1) is an enzyme that catalyzes the interconversion of pyruvate and acetyl-CoA. It is also called pyruvate:ferredoxin oxidoreductase (PFOR).
The relevant equilibrium catalysed by PFOR is:
The 3 substrates of this enzyme are pyruvate, CoA, and oxidized ferredoxin, whereas its 3 products are acetyl-CoA, CO2, and reduced ferredoxin.
This enzyme participates in 4 metabolic pathways: pyruvate metabolism, propanoate metabolism, butanoate metabolism, and reductive carboxylate cycle (CO2 fixation).
Its major role is the extraction of reducing equivalents by the decarboxylation. In aerobic organisms, this conversion is catalysed by pyruvate dehydrogenase, also uses thiamine pyrophosphate (TPP) but relies on lipoate as the electron acceptor. Unlike the aerobic enzyme complex PFOR transfers reducing equivalents to flavins or iron-sulflur clusters. This process links glycolysis to the Wood–Ljungdahl pathway.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with an iron-sulfur protein as acceptor. [1] The systematic name of this enzyme class is pyruvate:ferredoxin 2-oxidoreductase (CoA-acetylating). Other names in common use include:
PFOR adopts a dimeric structure, while each monomeric subunit is composed of one or multiple chain(s) of polypeptides. [1] Each monomeric subunit of PFOR consists of six domains binding one TPP molecule and three [4Fe-4S] clusters. [2]
An PFOR reaction starts with the nucleophilic attack of C2 of TPP on the 2-oxo carbon of pyruvate, which forms a lactyl-TPP adduct. Next, the lactyl-TPP adduct releases the CO2 moiety, forming an anionic intermediate, which then transfer an electron to a [4Fe-4S] cluster. These steps lead to a stable radical intermediate that can be observed by electron paramagnetic resonance (EPR) experiments. The radical intermediate reacts with a CoA molecule, transfers another electron from the radical intermediate to a [4Fe-4S] cluster and forms an acetyl-CoA product. [3]
The citric acid cycle—also known as the Krebs cycle, Szent–Györgyi–Krebs cycle, or TCA cycle —is a series of biochemical reactions to release the energy stored in nutrients through the oxidation of acetyl-CoA derived from carbohydrates, fats, proteins, and alcohol. The chemical energy released is available in the form of ATP. The Krebs cycle is used by organisms that respire to generate energy, either by anaerobic respiration or aerobic respiration. In addition, the cycle provides precursors of certain amino acids, as well as the reducing agent NADH, that are used in numerous other reactions. Its central importance to many biochemical pathways suggests that it was one of the earliest components of metabolism. Even though it is branded as a "cycle", it is not necessary for metabolites to follow only one specific route; at least three alternative segments of the citric acid cycle have been recognized.
The green sulfur bacteria are a phylum, Chlorobiota, of obligately anaerobic photoautotrophic bacteria that metabolize sulfur.
Ferredoxins are iron–sulfur proteins that mediate electron transfer in a range of metabolic reactions. The term "ferredoxin" was coined by D.C. Wharton of the DuPont Co. and applied to the "iron protein" first purified in 1962 by Mortenson, Valentine, and Carnahan from the anaerobic bacterium Clostridium pasteurianum.
Pyruvate carboxylase (PC) encoded by the gene PC is an enzyme of the ligase class that catalyzes the physiologically irreversible carboxylation of pyruvate to form oxaloacetate (OAA).
Pyruvate dehydrogenase is an enzyme that catalyzes the reaction of pyruvate and a lipoamide to give the acetylated dihydrolipoamide and carbon dioxide. The conversion requires the coenzyme thiamine pyrophosphate.
Nitazoxanide, sold under the brand name Alinia among others, is a broad-spectrum antiparasitic and broad-spectrum antiviral medication that is used in medicine for the treatment of various helminthic, protozoal, and viral infections. It is indicated for the treatment of infection by Cryptosporidium parvum and Giardia lamblia in immunocompetent individuals and has been repurposed for the treatment of influenza. Nitazoxanide has also been shown to have in vitro antiparasitic activity and clinical treatment efficacy for infections caused by other protozoa and helminths; evidence as of 2014 suggested that it possesses efficacy in treating a number of viral infections as well.
Formate dehydrogenases are a set of enzymes that catalyse the oxidation of formate to carbon dioxide, donating the electrons to a second substrate, such as NAD+ in formate:NAD+ oxidoreductase (EC 1.17.1.9) or to a cytochrome in formate:ferricytochrome-b1 oxidoreductase (EC 1.2.2.1). This family of enzymes has attracted attention as inspiration or guidance on methods for the carbon dioxide fixation, relevant to global warming.
In enzymology, a malate dehydrogenase (oxaloacetate-decarboxylating) (EC 1.1.1.38) is an enzyme that catalyzes the chemical reaction below
In enzymology, a 2-oxoglutarate synthase (EC 1.2.7.3) is an enzyme that catalyzes the chemical reaction
In enzymology, carbon monoxide dehydrogenase (CODH) (EC 1.2.7.4) is an enzyme that catalyzes the chemical reaction
In enzymology, a carbon-monoxide dehydrogenase (ferredoxin) (EC 1.2.7.4) is an enzyme that catalyzes the chemical reaction
In enzymology, an indolepyruvate ferredoxin oxidoreductase (EC 1.2.7.8) is an enzyme that catalyzes the chemical reaction
A pyruvate oxidase is basically an enzyme that speeds up a chemical reaction.
Butyryl-CoA is an organic coenzyme A-containing derivative of butyric acid. It is a natural product found in many biological pathways, such as fatty acid metabolism, fermentation, and 4-aminobutanoate (GABA) degradation. It mostly participates as an intermediate, a precursor to and converted from crotonyl-CoA. This interconversion is mediated by butyryl-CoA dehydrogenase.
Pyruvate dehydrogenase (lipoamide) alpha 2, also known as pyruvate dehydrogenase E1 component subunit alpha, testis-specific form, mitochondrial or PDHE1-A type II, is an enzyme that in humans is encoded by the PDHA2 gene.
Flavoprotein pyridine nucleotide cytochrome reductases catalyse the interchange of reducing equivalents between one-electron carriers and the two-electron-carrying nicotinamide dinucleotides. The enzymes include ferredoxin-NADP+ reductases, plant and fungal NAD(P)H:nitrate reductases, cytochrome b5 reductases, cytochrome P450 reductases, sulphite reductases, nitric oxide synthases, phthalate dioxygenase reductase, and various other flavoproteins.
Ferredoxin-thioredoxin reductase EC 1.8.7.2, systematic name ferredoxin:thioredoxin disulfide oxidoreductase, is a [4Fe-4S] protein that plays an important role in the ferredoxin/thioredoxin regulatory chain. It catalyzes the following reaction:
Oxalate oxidoreductases (EC 1.2.7.10) (OOR) are a relatively recently discovered group of enzymes that break down oxalate, a problematic molecule nutritionally. The first one to have been characterized has the systematic name oxalate:ferredoxin oxidoreductase. This enzyme catalyses the following chemical reaction:
In enzymology, an aldehyde ferredoxin oxidoreductase (EC 1.2.7.5) is an enzyme that catalyzes the chemical reaction
In enzymology, a formylmethanofuran dehydrogenase (EC 1.2.99.5) is an enzyme that catalyzes the chemical reaction:
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