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Microsomal P450
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 Mitoch ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Cytochrome P450
Cytochromes P450 (P450s or CYPs) are a Protein superfamily, superfamily of enzymes containing heme as a cofactor (biochemistry), cofactor that mostly, but not exclusively, function as monooxygenases. However, they are not omnipresent; for example, they have not been found in ''Escherichia coli''. In mammals, these enzymes oxidize steroids, fatty acids, xenobiotics, and participate in many biosyntheses. By hydroxylation, CYP450 enzymes convert xenobiotics into hydrophilic derivatives, which are more readily excreted. P450s are, in general, the terminal oxidase enzymes in electron transfer chains, broadly categorized as P450-containing systems. The term "P450" is derived from the spectrophotometry, spectrophotometric peak at the wavelength of the absorption spectroscopy, absorption maximum of the enzyme (450 nanometre, nm) when it is in the redox, reduced state and complexed with carbon monoxide. Most P450s require a protein partner to deliver one or more electrons to reduc ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Sterol 14-demethylase
In enzymology, a sterol 14-demethylase () is an enzyme of the cytochrome P450 (CYP) superfamily. It is any member of the CYP51 family. It catalyzes a chemical reaction such as: : obtusifoliol + 3 O2 + 3 NADPH + 3 H+ \rightleftharpoons 4alpha-methyl-5alpha-ergosta-8,14,24(28)-trien-3beta-ol + formate + 3 NADP+ + 4 H2O The 4 substrates here are obtusifoliol, O2, NADPH, and H+, whereas its 4 products are 4alpha-methyl-5alpha-ergosta-8,14,24(28)-trien-3beta-ol, formate, NADP+, and H2O. Although the lanosterol 14α-demethylase is present in a wide variety of organisms, the enzyme is studied primarily in the context of fungi, where it plays an essential role in mediating membrane permeability. In fungi, CYP51 catalyzes the demethylation of lanosterol to create an important precursor that is eventually converted into ergosterol. This steroid then makes its way throughout the cell, where it alters the permeability and rigidity of plasma membranes much as cholesterol does in anima ... [...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 Electron transport chain#Quinone carriers, 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-related biphenyl chemical compounds. References External linksType strain of ''Sphingomonas paucimobilis'' at Bac''Dive'' - the Bacterial Diversity Metadatabase Sphingomonas, paucimobilis Pathogenic bacteria Bacteria described in 1977 {{Sphingomonadales-stub ... [...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, an ... [...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 factitious air, among others, is a chemical compound, an Nitrogen oxide, oxide of nitrogen with the Chemical formula, formula . At room temperature, it is a colourless Flammability#Definitions, non-flammable gas, and has a slightly sweet scent and taste. At elevated temperatures, nitrous oxide is a powerful Oxidising agent, oxidiser similar to molecular oxygen. Nitrous oxide has significant Nitrous oxide (medication), medical uses, especially in surgery and dentistry, for its Anesthesia, anaesthetic and Analgesic, pain-reducing effects, and it is on the WHO Model List of Essential Medicines, World Health Organization's List of Essential Medicines. Its colloquial name, "laughing gas", coined by Humphry Davy, describes the Euphoria, euphoric effects upon inhaling it, which cause it to be used as a recreational drug inducing a brief "Dissociative, high". When abused chronically ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Nitric Oxide
Nitric oxide (nitrogen oxide, nitrogen monooxide, 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 (•N=O or •NO). Nitric oxide is also a heteronuclear diatomic molecule, a class of molecules whose study spawned early modern theories of chemical bonding. An important intermediate in 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 processes. It was proclaimed the " Molecule of the Year" in 1992. The 1998 Nobel Prize in Physiology or Medicine was awarded for discovering nitric oxide's role as a cardiovascular signalling molecule. Its impact extends beyond biology, with applications in medicine, such as the development of ... [...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-d ... [...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 chemistry, chemical transformation of one set of chemical substances to another. When chemical reactions occur, the atoms are rearranged and the reaction is accompanied by an Gibbs free energy, ... : 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 iron (Fe) atom at its core, as a cofactor. They are involved in the 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 ... [...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. Gene Human POR gene has 16 exons and the exons 2-16 code for a 677-amino acid POR protein (NCBI NP_000932.2). There is a single copy of 50 kb POR gene (NCBI NM_000941.2) in humans on chromosome 7 (7q11.23). Paralogs of POR include nitric oxide synthase (), NADPH:sulfite reductase (), and methionine synthase reductase (). Protein structure The 3D crystal structure of human POR has been determined.); The molecule is composed of four structural domains: the FMN-binding domain, the connecting domain, the FAD-binding domain, and NADPH-binding domain. The FMN-binding domain is similar to the structure of FMN-containing prot ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
