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Clostridium Sticklandii
''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. ''A. sticklandii'' is not pathogenic in humans. Biology and biochemistry ''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. Selenoproteins can be found in the genome of ''A. sticklandii''. One such selenoprotein, glycine reductase A was first identified in ''A. sticklandii''. ''A. sticklandii'' use ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Deutsche Sammlung Von Mikroorganismen Und Zellkulturen
The Leibniz Institute DSMZ - German Collection of Microorganisms and Cell Cultures GmbH (German: ''Leibniz-Institut DSMZ-Deutsche Sammlung von Mikroorganismen und Zellkulturen GmbH''), located in Braunschweig, is a research infrastructure in the Leibniz Association. Also the DSMZ is the world's most diverse collection of bioresources (status 2021: 75,000 bioresources). These include microorganisms (including more than 32,000 bacterial strains, 690 archaeal strains, 7,000 strains of yeasts and fungi) as well as more than 840 human and animal cell cultures, over 1. 500 plant viruses, over 940 bacteriophages, and 250 plasmids (status 2021). Since 2010, the scientific director of the Leibniz Institute DSMZ has been Jörg Overmann, a microbiologist with a PhD. He holds a professorship in microbiology at the Technical University of Braunschweig. Since August 2018, he has led the institute in a dual leadership with Bettina Fischer as administrative director. History Structure ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Pyrophosphatase
Pyrophosphatases, also known as diphosphatases, are acid anhydride hydrolases that act upon diphosphate bonds. Examples include: * Inorganic pyrophosphatase, which acts upon the free pyrophosphate ion * Tobacco acid pyrophosphatase, which catalyses the hydrolysis of a phosphoric ester * Various organic pyrophosphatases, which act upon organic molecules with the pyrophosphate group (but excluding triphosphatases that act on the final bond): ** Thiamine pyrophosphatase In enzymology, a nucleoside-diphosphatase () is an enzyme that catalyzes the chemical reaction :a nucleoside diphosphate + H2O \rightleftharpoons a nucleotide + phosphate Thus, the two substrates of this enzyme are nucleoside diphosphate and ... See also * References External links * EC 3.6.1 {{3.6-enzyme-stub ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Peptostreptococcaceae
The Peptostreptococcaceae are a family of Gram-positive bacteria in the class Clostridia. Several members of the Peptostreptococcaceae are well known inhabitants of the digestive tract. Microbiome studies of animal feces have corroborated this. Notably, an unclassified group of Peptostreptococcaceae has been reported making up a significant portion of the microbial community in domestic cats, while other studies have not found a significant presence of Peptostreptococcaceae. '' Clostridioides difficile'' is a notable human pathogen in this family. Peptostreptococcaceae have been of interest for several other bowel diseases as biological marker or causative agent. Decreased abundance has been reported for Crohn's disease, while the genus '' Peptostreptococcus'' appears to be more common in patients diagnosed with colorectal cancer Colorectal cancer (CRC), also known as bowel cancer, colon cancer, or rectal cancer, is the development of cancer from the colon or rectum ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Clostridioides Difficile
''Clostridioides difficile'' ( syn. ''Clostridium difficile'') is a bacterium that is well known for causing serious diarrheal infections, and may also cause colon cancer. Also known as ''C. difficile'', or ''C. diff'' (), is Gram-positive species of spore-forming bacteria. ''Clostridioides'' spp. are anaerobic, motile bacteria, ubiquitous in nature and especially prevalent in soil. Its vegetative cells are rod-shaped, pleomorphic, and occur in pairs or short chains. Under the microscope, they appear as long, irregular (often drumstick- or spindle-shaped) cells with a bulge at their terminal ends (forms subterminal spores). Under Gram staining, ''C. difficile'' cells are Gram-positive and show optimum growth on blood agar at human body temperatures in the absence of oxygen. ''C. difficile'' is catalase- and superoxide dismutase-negative, and produces up to three types of toxins: enterotoxin A, cytotoxin B and Clostridioides difficile transferase (CDT). Under stress conditio ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Glutathione Peroxidase
Glutathione peroxidase (GPx) () is the general name of an enzyme family with peroxidase activity whose main biological role is to protect the organism from oxidative damage. The biochemical function of glutathione peroxidase is to reduce lipid hydroperoxides to their corresponding alcohols and to reduce free hydrogen peroxide to water. Isozymes Several isozymes are encoded by different genes, which vary in cellular location and substrate specificity. Glutathione peroxidase 1 (GPx1) is the most abundant version, found in the cytoplasm of nearly all mammalian tissues, whose preferred substrate is hydrogen peroxide. Glutathione peroxidase 4 (GPx4) has a high preference for lipid hydroperoxides; it is expressed in nearly every mammalian cell, though at much lower levels. Glutathione peroxidase 2 is an intestinal and extracellular enzyme, while glutathione peroxidase 3 is extracellular, especially abundant in plasma. So far, eight different isoforms of glutathione peroxidase ( ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Rubrerythrin
Rubrerythrin (RBR) is a non-heme iron-containing metalloprotein involved in oxidative stress tolerance within anaerobic bacteria. It contains a di-iron active site, where peroxide is reduced into two water molecules, and a mono-iron rubredoxin-like domain thought to be involved in electron transfer. A majority of known RBR families are utilized as peroxide "scavengers" to defend organisms against oxidative stress. Function As a member of the Ferritin-like superfamily, RBRs primary function is iron storage and detoxification. Rubrerythrins utilize their di-iron centers to bind with reactive oxygen species such as Hydrogen Peroxide, further reducing them into water. RBR reduction is theorized as a particularly important adaptation that occurred in response to the Great Oxygenation event, increasing defensive fitness of all cells exposed to relatively high levels of oxygen and similar byproducts. Although primarily studied within anaerobic bacteria, RBRs have been discovered in mu ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Superoxide Reductase
Superoxide reductase is an enzyme that catalyzes the conversion of highly reactive and toxic superoxide (O2−) into less toxic hydrogen peroxide (H2O2): :reduced rubredoxin + O2− + 2 H+ \rightleftharpoons rubredoxin + H2O2 :Fe2+ + O2− + 2 H+ \rightleftharpoons Fe3++ H2O2 Hydrogen peroxide in turn is reduced to water by rubrerythrin. The 3 substrates of this enzyme are reduced rubredoxin, superoxide, and H+, whereas its two products are rubredoxin and H2O2. This enzyme belongs to the family of oxidoreductases, specifically those acting on superoxide as acceptor (only sub-subclass identified to date). The systematic name of this enzyme class is rubredoxin:superoxide oxidoreductase. Other names in common use include neelaredoxin, and desulfoferrodoxin. Structural studies , 9 structures A structure is an arrangement and organization of interrelated elements in a material object or system, or the object or system so organized. Material structures include man-made object ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Glycine Synthase
The glycine cleavage system (GCS) is also known as the glycine decarboxylase complex or GDC. The system is a series of enzymes that are triggered in response to high concentrations of the amino acid glycine. The same set of enzymes is sometimes referred to as glycine synthase when it runs in the reverse direction to form glycine. The glycine cleavage system is composed of four proteins: the T-protein, P-protein, L-protein, and H-protein. They do not form a stable complex, so it is more appropriate to call it a "system" instead of a "complex". The H-protein is responsible for interacting with the three other proteins and acts as a shuttle for some of the intermediate products in glycine decarboxylation. In both animals and plants the glycine cleavage system is loosely attached to the inner membrane of the mitochondria. Mutations in this enzymatic system are linked with glycine encephalopathy. Components Function In plants, animals and bacteria the glycine cleavage system cataly ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
V-ATPase
Vacuolar-type ATPase (V-ATPase) is a highly conserved evolutionarily ancient enzyme with remarkably diverse functions in eukaryotic organisms. V-ATPases acidify a wide array of intracellular organelles and pumps protons across the plasma membranes of numerous cell types. V-ATPases couple the energy of ATP hydrolysis to proton transport across intracellular and plasma membranes of eukaryotic cells. It is generally seen as the polar opposite of ATP synthase because ATP synthase is a proton channel that uses the energy from a proton gradient to produce ATP. V-ATPase however, is a proton pump that uses the energy from ATP hydrolysis to produce a proton gradient. The Archaea-type ATPase (A-ATPase) is a related group of ATPases found in archaea that often work as an ATP synthase. It forms a clade V/A-ATPase with V-ATPase. Most members of either group shuttle protons (), but a few members have evolved to use sodium ions () instead. Roles played by V-ATPases V-ATPases are foun ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Anaerobic Organism
An anaerobic organism or anaerobe is any organism that does not require molecular oxygen for growth. It may react negatively or even die if free oxygen is present. In contrast, an aerobic organism (aerobe) is an organism that requires an oxygenated environment. Anaerobes may be unicellular (e.g. protozoans, bacteria) or multicellular. Most fungi are obligate aerobes, requiring oxygen to survive. However, some species, such as the Chytridiomycota that reside in the rumen of cattle, are obligate anaerobes; for these species, anaerobic respiration is used because oxygen will disrupt their metabolism or kill them. Deep waters of the ocean are a common anoxic environment. First observation In his letter of 14 June 1680 to The Royal Society, Antonie van Leeuwenhoek described an experiment he carried out by filling two identical glass tubes about halfway with crushed pepper powder, to which some clean rain water was added. Van Leeuwenhoek sealed one of the glass tubes using a flame an ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
F-ATPase
F-ATPase, also known as F-Type ATPase, is an ATPase/ synthase found in bacterial plasma membranes, in mitochondrial inner membranes (in oxidative phosphorylation, where it is known as Complex V), and in chloroplast thylakoid membranes. It uses a proton gradient to drive ATP synthesis by allowing the passive flux of protons across the membrane down their electrochemical gradient and using the energy released by the transport reaction to release newly formed ATP from the active site of F-ATPase. Together with V-ATPases and A-ATPases, F-ATPases belong to superfamily of related rotary ATPases. F-ATPase consists of two domains: * the Fo domain, which is integral in the membrane and is composed of 3 different types of integral proteins classified as a, b and c. * the F1, which is peripheral (on the side of the membrane that the protons are moving into). F1 is composed of 5 polypeptide units α3β3γδε that bind to the surface of the Fo domain. F-ATPases usually work as ATP syn ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
