Acetoanaerobium sticklandii | |
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Scientific classification ![]() | |
Domain: | Bacteria |
Phylum: | Bacillota |
Class: | Clostridia |
Order: | Eubacteriales |
Family: | Peptostreptococcaceae |
Genus: | Acetoanaerobium |
Species: | A. sticklandii |
Binomial name | |
Acetoanaerobium sticklandii (Stadtman and McClung 1957) Galperin et al. 2016 [1] | |
Synonyms | |
Clostridium sticklandiiStadtman and McClung 1957 [1] Contents |
Acetoanaerobium sticklandii is an anaerobic, motile, gram-positive bacterium. It was first isolated in 1954 from the black mud of the San Francisco Bay Area by T.C. Stadtman, who also named the species. [2] A. sticklandii is not pathogenic in humans.
Acetoanaerobium sticklandii ferment amino acids by using the Stickland reaction, which couples the oxidation of one amino acid and the reduction of another. L.H. Stickland described this process in 1934. The enzymes in the Stickland reaction are D-proline reductase (an electron acceptor) and Glycine reductase. A. sticklandii preferentially utilize threonine, arginine, serine, cysteine, proline, and glycine during the growth phase and lysine during the stationary phase, while excreting glutamate, aspartate and alanine.[ citation needed ]
Selenoproteins can be found in the genome of A. sticklandii. One such selenoprotein, glycine reductase A was first identified in A. sticklandii. A. sticklandii uses a total of eight of these selenoproteins. One of which, PrdC, was not previously thought to be a selenoprotein. PrdC, which is similar to RnfC in other species, is found within the D-proline reductase operon. The D-proline reductase operon is responsible for the reductive ring cleavage of D-proline into 5-aminovalerate. 5-aminovalerate is excreted by Cl. sticklandii.[ citation needed ]
Although energy conservation in A. sticklandii is achieved through substrate level phosphorylation, it can be achieved via electron-transport phosphorylation as well. The Rnf complex, a Na+-dependent F-ATPase, V-ATPase, and a membrane-bound Pyrophosphatase serve as methods to conserve energy through electron-transport phosphorylation.[ citation needed ]
On another interesting note, A. sticklandii have two carbon dioxide fixation pathways, Wood-Ljundgahl and Glycine synthase/glycine reductase pathways. It is an oddity to find both of these methods of carbon dioxide fixation simultaneously. Only four other bacterial species have been observed to contain both of these pathways. Although, A. sticklandii has the ability to utilize both pathways, it has not been determined if they do utilize both pathways at the same time.[ citation needed ]
Although it is considered an obligate anaerobe, A. sticklandii has genes that allow for the bacterium to be cultivated in aerobic conditions. Some of the proteins made by A. sticklandii that allow for the repair of damage from oxygen exposure include Mn-superoxide dismutase [3] and Superoxide reductase, alkyl hydroperoxide reductase, [4] rubrerythrin, [5] Glutathione peroxidases, seleno-peroxiredoxin, thioredoxin-dependent peroxidase, and sulfoxide reductases A and B.
Acetoanaerobium sticklandii has a genome that consists of one circular chromosome. On this chromosome are 2,715,461 base pairs. Of these base pairs there are 2573 coding sequences with only 2.1% of the genome repeated. A. sticklandii shares the highest number of genes that are homologous with Clostridioides difficile (a pathogenic species in the Peptostreptococcaceae) and with two members of the genus Alkaliphilus .[ citation needed ]
Antioxidants are compounds that inhibit oxidation, a chemical reaction that can produce free radicals. Autoxidation leads to degradation of organic compounds, including living matter. Antioxidants are frequently added to industrial products, such as polymers, fuels, and lubricants, to extend their usable lifetimes. Food are also treated with antioxidants to forestall spoilage, in particular the rancidification of oils and fats. In cells, antioxidants such as glutathione, mycothiol or bacillithiol, and enzyme systems like superoxide dismutase, can prevent damage from oxidative stress.
Oxidative phosphorylation or electron transport-linked phosphorylation or terminal oxidation is the metabolic pathway in which cells use enzymes to oxidize nutrients, thereby releasing chemical energy in order to produce adenosine triphosphate (ATP). In eukaryotes, this takes place inside mitochondria. Almost all aerobic organisms carry out oxidative phosphorylation. This pathway is so pervasive because it releases more energy than alternative fermentation processes such as anaerobic glycolysis.
Selenocysteine is the 21st proteinogenic amino acid. Selenoproteins contain selenocysteine residues. Selenocysteine is an analogue of the more common cysteine with selenium in place of the sulfur.
The cytochrome complex, or cyt c, is a small hemeprotein found loosely associated with the inner membrane of the mitochondrion where it plays a critical role in cellular respiration. It transfers electrons between Complexes III and IV. Cytochrome c is highly water-soluble, unlike other cytochromes. It is capable of undergoing oxidation and reduction as its iron atom converts between the ferrous and ferric forms, but does not bind oxygen. It also plays a major role in cell apoptosis. In humans, cytochrome c is encoded by the CYCS gene.
In molecular biology a selenoprotein is any protein that includes a selenocysteine amino acid residue. Among functionally characterized selenoproteins are five glutathione peroxidases (GPX) and three thioredoxin reductases, (TrxR/TXNRD) which both contain only one Sec. Selenoprotein P is the most common selenoprotein found in the plasma. It is unusual because in humans it contains 10 Sec residues, which are split into two domains, a longer N-terminal domain that contains 1 Sec, and a shorter C-terminal domain that contains 9 Sec. The longer N-terminal domain is likely an enzymatic domain, and the shorter C-terminal domain is likely a means of safely transporting the very reactive selenium atom throughout the body.
Obligate anaerobes are microorganisms killed by normal atmospheric concentrations of oxygen (20.95% O2). Oxygen tolerance varies between species, with some species capable of surviving in up to 8% oxygen, while others lose viability in environments with an oxygen concentration greater than 0.5%.
In molecular biology, biosynthesis is a multi-step, enzyme-catalyzed process where substrates are converted into more complex products in living organisms. In biosynthesis, simple compounds are modified, converted into other compounds, or joined to form macromolecules. This process often consists of metabolic pathways. Some of these biosynthetic pathways are located within a single cellular organelle, while others involve enzymes that are located within multiple cellular organelles. Examples of these biosynthetic pathways include the production of lipid membrane components and nucleotides. Biosynthesis is usually synonymous with anabolism.
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.
Drug metabolism is the metabolic breakdown of drugs by living organisms, usually through specialized enzymatic systems. More generally, xenobiotic metabolism is the set of metabolic pathways that modify the chemical structure of xenobiotics, which are compounds foreign to an organism's normal biochemistry, such as any drug or poison. These pathways are a form of biotransformation present in all major groups of organisms and are considered to be of ancient origin. These reactions often act to detoxify poisonous compounds. The study of drug metabolism is called pharmacokinetics.
Stickland fermentation or The Stickland Reaction is the name for a chemical reaction that involves the coupled oxidation and reduction of amino acids to organic acids. The electron donor amino acid is oxidised to a volatile carboxylic acid one carbon atom shorter than the original amino acid. For example, alanine with a three carbon chain is converted to acetate with two carbons. The electron acceptor amino acid is reduced to a volatile carboxylic acid the same length as the original amino acid. For example, glycine with two carbons is converted to acetate.
Methanosarcina acetivorans is a versatile methane producing microbe which is found in such diverse environments as oil wells, trash dumps, deep-sea hydrothermal vents, and oxygen-depleted sediments beneath kelp beds. Only M. acetivorans and microbes in the genus Methanosarcina use all three known metabolic pathways for methanogenesis. Methanosarcinides, including M. acetivorans, are also the only archaea capable of forming multicellular colonies, and even show cellular differentiation. The genome of M. acetivorans is one of the largest archaeal genomes ever sequenced. Furthermore, one strain of M. acetivorans, M. a. C2A, has been identified to possess an F-type ATPase along with an A-type ATPase.
Nitrate reductases are molybdoenzymes that reduce nitrate to nitrite. This reaction is critical for the production of protein in most crop plants, as nitrate is the predominant source of nitrogen in fertilized soils.
Amino acid synthesis is the set of biochemical processes by which the amino acids are produced. The substrates for these processes are various compounds in the organism's diet or growth media. Not all organisms are able to synthesize all amino acids. For example, humans can synthesize 11 of the 20 standard amino acids. These 11 are called the non-essential amino acids).
Betaine reductase is an enzyme that catalyzes the chemical reaction
In enzymology, a D-proline reductase (dithiol) is an enzyme that catalyzes the chemical reaction
In enzymology, a glycine reductase (EC 1.21.4.2) is an enzyme that catalyzes the chemical reaction
In enzymology, a 2,4-diaminopentanoate dehydrogenase (EC 1.4.1.12) is an enzyme that catalyzes the chemical reaction
In enzymology, D-lysine 5,6-aminomutase is an enzyme that catalyzes the chemical reaction
Pyocyanin (PCN−) is one of the many toxic compounds produced and secreted by the Gram negative bacterium Pseudomonas aeruginosa. Pyocyanin is a blue secondary metabolite, turning red below pH 4.9, with the ability to oxidise and reduce other molecules and therefore kill microbes competing against P. aeruginosa as well as mammalian cells of the lungs which P. aeruginosa has infected during cystic fibrosis. Since pyocyanin is a zwitterion at blood pH, it is easily able to cross the cell membrane. There are three different states in which pyocyanin can exist: oxidized (blue), monovalently reduced (colourless) or divalently reduced (red). Mitochondria play an important role in the cycling of pyocyanin between its redox states. Due to its redox-active properties, pyocyanin generates reactive oxygen species.
The Arc system is a two-component system found in some bacteria that regulates gene expression in faculatative anaerobes such as Escheria coli. Two-component system means that it has a sensor molecule and a response regulator. Arc is an abbreviation for Anoxic Redox Control system. Arc systems are instrumental in maintaining energy metabolism during transcription of bacteria. The ArcA response regulator looks at growth conditions and expresses genes to best suit the bacteria. The Arc B sensor kinase, which is a tripartite protein, is membrane bound and can autophosphorylate.