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P450-containing Systems
Any enzyme system that includes cytochrome P450 protein or domain can be called a P450-containing system. P450 enzymes usually function as a terminal oxidase in multicomponent electron-transfer chains, called P450-containing monooxygenase systems, although self-sufficient, non-monooxygenase P450s have been also described. All known P450-containing monooxygenase systems share common structural and functional domain architecture. Apart from the cytochrome itself, these systems contain one or more fundamental redox domains: FAD-containing flavoprotein or domain, FMN domain, ferredoxin and cytochrome ''b''5. These ubiquitous redox domains, in various combinations, are widely distributed in biological systems. FMN domain, ferredoxin or cytochrome ''b''5 transfer electrons between the flavin reductase (protein or domain) and P450. While P450-containing systems are found throughout all kingdoms of life, some organisms lack one or more of these redox domains. FR/Fd/P450 systems Mitocho ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Cytochrome P450
Cytochromes P450 (CYPs) are a Protein superfamily, superfamily of enzymes containing heme as a cofactor (biochemistry), cofactor that functions as monooxygenases. In mammals, these proteins oxidize steroids, fatty acids, and xenobiotics, and are important for the clearance (pharmacology), clearance of various compounds, as well as for hormone synthesis and breakdown. In 1963, Ronald W. Estabrook, Estabrook, David Y. Cooper, Cooper, and Otto Rosenthal, Rosenthal described the role of CYP as a catalyst in steroid hormone synthesis and drug metabolism. In plants, these proteins are important for the biosynthesis of secondary metabolite, defensive compounds, fatty acids, and hormones. CYP enzymes have been identified in all kingdom (biology), kingdoms of life: animals, plants, fungus, fungi, protists, bacteria, and archaea, as well as in viruses. However, they are not omnipresent; for example, they have not been found in ''Escherichia coli''. , more than 300,000 distinct CYP proteins ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Adrenodoxin
Adrenal ferredoxin (also adrenodoxin (ADX), adrenodoxin, mitochondrial, hepatoredoxin, ferredoxin-1 (FDX1)) is a protein that in humans is encoded by the ''FDX1'' gene. In addition to the expressed gene at this chromosomal locus (11q22), there are pseudogenes located on chromosomes 20 and 21. Function Adrenodoxin is a small iron-sulfur protein that can accept and carry a single electron. Adrenodoxin functions as an electron transfer protein in the mitochondrial cytochrome P450 systems. The first enzyme in this system is adrenodoxin reductase that carries an FAD. FAD can be reduced by two electrons donated from coenzyme NADPH. These two electrons are transferred one a time to adrenodoxin. Adrenodoxin in return reduces mitochondrial cytochrome P450. This particular oxidation/reduction system is involved in the synthesis of steroid hormones in steroidogenic tissues. In addition, similar systems also function in vitamin D and bile acid Bile acids are steroid acids found predomina ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Sphingomonas Paucimobilis
Sphingomonas paucimobilis is a strictly aerobic Gram-negative bacterium that has a single polar flagellum with slow motility. The cell size is around 0.7 x 1.4 μm. It is usually found in soil. As with the other members of the genus, its biochemistry is remarkable in possession of ubiquinone 10 as its major respiratory quinone, and of glycosphingolipids instead of lipopolysaccharides in its cell envelope. It has been implicated in various types of clinical infections. ''S. paucimobilis'' is able to degrade lignin Lignin is a class of complex organic polymers that form key structural materials in the support tissues of most plants. Lignins are particularly important in the formation of cell walls, especially in wood and bark, because they lend rigidity ...-related biphenyl chemical compounds. References External linksType strain of ''Sphingomonas paucimobilis'' at Bac''Dive'' - the Bacterial Diversity Metadatabase paucimobilis Bacteria described in 1977 {{Sp ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Bacillus Subtilis
''Bacillus subtilis'', known also as the hay bacillus or grass bacillus, is a Gram-positive, catalase-positive bacterium, found in soil and the gastrointestinal tract of ruminants, humans and marine sponges. As a member of the genus ''Bacillus'', ''B. subtilis'' is rod-shaped, and can form a tough, protective endospore, allowing it to tolerate extreme environmental conditions. ''B. subtilis'' has historically been classified as an obligate aerobe, though evidence exists that it is a facultative anaerobe. ''B. subtilis'' is considered the best studied Gram-positive bacterium and a model organism to study bacterial chromosome replication and cell differentiation. It is one of the bacterial champions in secreted enzyme production and used on an industrial scale by biotechnology companies. Description ''Bacillus subtilis'' is a Gram-positive bacterium, rod-shaped and catalase-positive. It was originally named ''Vibrio subtilis'' by Christian Gottfried Ehrenberg, and renamed ''B ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Fatty-acid Peroxygenase
Fatty-acid peroxygenase (, ''fatty acid hydroxylase (ambiguous)'', ''P450 peroxygenase'', ''CYP152A1'', ''P450BS'', ''P450SPalpha'') is an enzyme with systematic name ''fatty acid:hydroperoxide oxidoreductase (RH-hydroxylating)''. This enzyme catalyses the following chemical reaction : fatty acid + H2O2 \rightleftharpoons 3- or 2-hydroxy fatty acid + H2O Fatty-acid peroxygenase is a cytosolic heme-thiolate In organic chemistry, a thiol (; ), or thiol derivative, is any organosulfur compound of the form , where R represents an alkyl or other organic substituent. The functional group itself is referred to as either a thiol group or a sulfhydryl grou ... protein. References External links * {{Portal bar, Biology, border=no EC 1.11.2 ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Nitrous Oxide
Nitrous oxide (dinitrogen oxide or dinitrogen monoxide), commonly known as laughing gas, nitrous, or nos, is a chemical compound, an oxide of nitrogen with the formula . At room temperature, it is a colourless non-flammable gas, and has a slightly sweet scent and taste. At elevated temperatures, nitrous oxide is a powerful oxidiser similar to molecular oxygen. Nitrous oxide has significant medical uses, especially in surgery and dentistry, for its anaesthetic and pain-reducing effects. Its colloquial name, "laughing gas", coined by Humphry Davy, is due to the euphoric effects upon inhaling it, a property that has led to its recreational use as a dissociative anaesthetic. It is on the World Health Organization's List of Essential Medicines. It is also used as an oxidiser in rocket propellants, and in motor racing to increase the power output of engines. Nitrous oxide's atmospheric concentration reached 333 parts per billion (ppb) in 2020, increasing at a rate of abo ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Nitric Oxide
Nitric oxide (nitrogen oxide or nitrogen monoxide) is a colorless gas with the formula . It is one of the principal oxides of nitrogen. Nitric oxide is a free radical: it has an unpaired electron, which is sometimes denoted by a dot in its chemical formula In chemistry, a chemical formula is a way of presenting information about the chemical proportions of atoms that constitute a particular chemical compound or molecule, using chemical element symbols, numbers, and sometimes also other symbols, ... (•N=O or •NO). Nitric oxide is also a heteronuclear diatomic molecule, a class of molecules whose study spawned early modern molecular orbital theory, theories of chemical bonding. An important Reaction intermediate, intermediate in chemical industry, industrial chemistry, nitric oxide forms in combustion systems and can be generated by lightning in thunderstorms. In mammals, including humans, nitric oxide is a signaling molecule in many physiological and pathological pro ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Fusarium Oxysporum
''Fusarium oxysporum'' (Schlecht as emended by Snyder and Hansen), an ascomycete fungus, comprises all the species, varieties and forms recognized by Wollenweber and Reinking within an infrageneric grouping called section Elegans. It is part of the family Nectriaceae. Although their predominant role in native soils may be as harmless or even beneficial plant endophytes or soil saprophytes, many strains within the ''F. oxysporum'' complex are soil borne pathogens of plants, especially in agricultural settings. Taxonomy While the species, as defined by Snyder and Hansen, has been widely accepted for more than 50 years, more recent work indicates this taxon is actually a genetically heterogeneous polytypic morphospecies, whose strains represent some of the most abundant and widespread microbes of the global soil microflora. Genome The ' family of transposable elements was first discovered by Daboussi ''et al.'', 1992 in several ''formae speciales'' and Davière ''et al.'', 2001 ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Denitrification
Denitrification is a microbially facilitated process where nitrate (NO3−) is reduced and ultimately produces molecular nitrogen (N2) through a series of intermediate gaseous nitrogen oxide products. Facultative anaerobic bacteria perform denitrification as a type of respiration that reduces oxidized forms of nitrogen in response to the oxidation of an electron donor such as organic matter. The preferred nitrogen electron acceptors in order of most to least thermodynamically favorable include nitrate (NO3−), nitrite (NO2−), nitric oxide (NO), nitrous oxide (N2O) finally resulting in the production of dinitrogen (N2) completing the nitrogen cycle. Denitrifying microbes require a very low oxygen concentration of less than 10%, as well as organic C for energy. Since denitrification can remove NO3−, reducing its leaching to groundwater, it can be strategically used to treat sewage or animal residues of high nitrogen content. Denitrification can leak N2O, which is an ozone ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Nitric Oxide Reductase (NAD(P), Nitrous Oxide-forming)
Nitric oxide reductase (NAD(P), nitrous oxide-forming) (, ''fungal nitric oxide reductase'', ''cytochrome P450nor'', ''NOR (ambiguous)'') is an enzyme with systematic name ''nitrous oxide:NAD(P) oxidoreductase''. This enzyme catalyses the following chemical reaction A chemical reaction is a process that leads to the IUPAC nomenclature for organic transformations, chemical transformation of one set of chemical substances to another. Classically, chemical reactions encompass changes that only involve the pos ... : N2O + NAD(P)+ + \rightleftharpoons 2 NO + NAD(P)H + H+ This enzyme is heme-thiolate protein (P450). References External links * {{Portal bar, Biology, border=no EC 1.7.1 ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Cytochrome ''b''5 Reductase
Cytochromes are redox-active proteins containing a heme, with a central Fe atom at its core, as a cofactor. They are involved in electron transport chain and redox catalysis. They are classified according to the type of heme and its mode of binding. Four varieties are recognized by the International Union of Biochemistry and Molecular Biology (IUBMB), cytochromes a, cytochromes b, cytochromes c and cytochrome d. Cytochrome function is linked to the reversible redox change from ferrous (Fe(II)) to the ferric (Fe(III)) oxidation state of the iron found in the heme core. In addition to the classification by the IUBMB into four cytochrome classes, several additional classifications such as cytochrome o and cytochrome P450 can be found in biochemical literature. History Cytochromes were initially described in 1884 by Charles Alexander MacMunn as respiratory pigments (myohematin or histohematin). In the 1920s, Keilin rediscovered these respiratory pigments and named them the c ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Cytochrome P450 Reductase
Cytochrome P450 reductase (; also known as NADPH:ferrihemoprotein oxidoreductase, NADPH:hemoprotein oxidoreductase, NADPH:P450 oxidoreductase, P450 reductase, POR, CPR, CYPOR) is a membrane-bound enzyme required for electron transfer from NADPH to cytochrome P450 and other heme proteins including heme oxygenase in the endoplasmic reticulum of the eukaryotic cell. Function In ''Bacillus megaterium'' and ''Bacillus subtilis'', POR is a C-terminal domain of CYP102, a single-polypeptide self-sufficient soluble P450 system (P450 is an N-terminal domain). The general scheme of electron flow in the POR/P450 system is: The definitive evidence for the requirement of POR in cytochrome-P450-mediated reactions came from the work of Lu, Junk and Coon, who dissected the P450-containing mixed function oxidase system into three constituent components: POR, cytochrome P450, and lipids. Since all microsomal P450 enzymes require POR for catalysis, it is expected that disruption of POR would ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
