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INOS
Nitric oxide synthases (NOSs) are a family of enzymes catalyzing the production of nitric oxide (NO) from L-arginine. NO is an important cellular signaling molecule. It helps modulate vascular tone, insulin secretion, airway tone, and peristalsis, and is involved in angiogenesis and neural development. It may function as a retrograde neurotransmitter. Nitric oxide is mediated in mammals by the calcium-calmodulin controlled isoenzymes eNOS (endothelial NOS) and nNOS (neuronal NOS). The inducible isoform, iNOS, involved in immune response, binds calmodulin at physiologically relevant concentrations, and produces NO as an immune defense mechanism, as NO is a free radical with an unpaired electron. It is the proximate cause of septic shock and may function in autoimmune disease. In the context of eukaryote biology, ''nitric oxide synthase'' refers to nitric-oxide synthase (NADPH) (), which catalyzes the reaction: * 2 L-arginine + 3 NADPH + 3 H+ + 4 O2 \rightleftharpoons 2 cit ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
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Biological Functions Of Nitric Oxide
Biological functions of nitric oxide are roles that nitric oxide plays within biology. Nitric oxide (nitrogen monoxide) is a molecule and chemical compound with chemical formula of N O. In mammals including humans, nitric oxide is a signaling molecule involved in several physiological and pathological processes. It is a powerful vasodilator with a half-life of a few seconds in the blood. Standard pharmaceuticals such as nitroglycerine and amyl nitrite are precursors to nitric oxide. Low levels of nitric oxide production are typically due to ischemic damage in the liver. As a consequence of its importance in neuroscience, physiology, and immunology, nitric oxide was proclaimed " Molecule of the Year" in 1992. Research into its function led to the 1998 Nobel Prize for elucidating the role of nitric oxide as a cardiovascular signalling molecule. Sources of nitric oxide Nitric oxide biosynthesis Platelet-derived factors, shear stress, acetylcholine, and cytokines stimulate the pr ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
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L-arginine
Arginine is the amino acid with the formula (H2N)(HN)CN(H)(CH2)3CH(NH2)CO2H. The molecule features a guanidino group appended to a standard amino acid framework. At physiological pH, the carboxylic acid is deprotonated (−CO2−) and both the amino and guanidino groups are protonated, resulting in a cation. Only the -arginine (symbol Arg or R) enantiomer is found naturally. Arg residues are common components of proteins. It is encoded by the codons CGU, CGC, CGA, CGG, AGA, and AGG. The guanidine group in arginine is the precursor for the biosynthesis of nitric oxide. Like all amino acids, it is a white, water-soluble solid. The one-letter symbol R was assigned to arginine for its phonetic similarity. History Arginine was first isolated in 1886 from yellow lupin seedlings by the German chemist Ernst Schulze and his assistant Ernst Steiger. He named it from the Greek ''árgyros'' (ἄργυρος) meaning "silver" due to the silver-white appearance of arginine nitrate crysta ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
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Endothelial NOS
Endothelial NOS (eNOS), also known as nitric oxide synthase 3 (NOS3) or constitutive NOS (cNOS), is an enzyme that in humans is encoded by the ''NOS3'' gene located in the 7q35-7q36 region of chromosome 7. This enzyme is one of three isoforms that synthesize nitric oxide (NO), a small gaseous and lipophilic molecule that participates in several biological processes. The other isoforms include neuronal nitric oxide synthase (nNOS), which is constitutively expressed in specific neurons of the brain and inducible nitric oxide synthase (iNOS), whose expression is typically induced in inflammatory diseases. eNOS is primarily responsible for the generation of NO in the vascular endothelium, a monolayer of flat cells lining the interior surface of blood vessels, at the interface between circulating blood in the lumen and the remainder of the vessel wall. NO produced by eNOS in the vascular endothelium plays crucial roles in regulating vascular tone, cellular proliferation, leukocyte ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
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Arginine
Arginine is the amino acid with the formula (H2N)(HN)CN(H)(CH2)3CH(NH2)CO2H. The molecule features a guanidinium, guanidino group appended to a standard amino acid framework. At physiological pH, the carboxylic acid is deprotonated (−CO2−) and both the amino and guanidino groups are protonated, resulting in a cation. Only the -arginine (symbol Arg or R) enantiomer is found naturally. Arg residues are common components of proteins. It is Genetic code, encoded by the DNA codon table, codons CGU, CGC, CGA, CGG, AGA, and AGG. The guanidine group in arginine is the Precursor (chemistry), precursor for the biosynthesis of nitric oxide. Like all amino acids, it is a white, water-soluble solid. The one-letter symbol R was assigned to arginine for its phonetic similarity. History Arginine was first isolated in 1886 from Lupinus luteus, yellow lupin seedlings by the German chemist Ernst Schulze (chemist), Ernst Schulze and his assistant Ernst Steiger. He named it from the Greek ''árg ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
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Enzymes
An enzyme () is a protein that acts as a biological catalyst by accelerating chemical reactions. The molecules upon which enzymes may act are called substrates, and the enzyme converts the substrates into different molecules known as products. Almost all metabolic processes in the cell need enzyme catalysis in order to occur at rates fast enough to sustain life. Metabolic pathways depend upon enzymes to catalyze individual steps. The study of enzymes is called ''enzymology'' and the field of pseudoenzyme analysis recognizes that during evolution, some enzymes have lost the ability to carry out biological catalysis, which is often reflected in their amino acid sequences and unusual 'pseudocatalytic' properties. Enzymes are known to catalyze more than 5,000 biochemical reaction types. Other biocatalysts include catalytic RNA molecules, also called ribozymes. They are sometimes described as a ''type'' of enzyme rather than being ''like'' an enzyme, but even in the d ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
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Flavin Mononucleotide
Flavin mononucleotide (FMN), or riboflavin-5′-phosphate, is a biomolecule produced from riboflavin (vitamin B2) by the enzyme riboflavin kinase and functions as the prosthetic group of various oxidoreductases, including NADH dehydrogenase, as well as a cofactor in biological blue-light photo receptors. During the catalytic cycle, various oxidoreductases induce reversible interconversions between the oxidized (FMN), semiquinone (FMNH•), and reduced (FMNH2) forms of the isoalloxazine core. FMN is a stronger oxidizing agent than NAD and is particularly useful because it can take part in both one- and two-electron transfers. In its role as blue-light photo receptor, (oxidized) FMN stands out from the 'conventional' photo receptors as the signaling state and not an E/Z isomerization. It is the principal form in which riboflavin is found in cells and tissues. It requires more energy to produce, but is more soluble than riboflavin. In cells, FMN occurs freely circulating but ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
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Superoxide
In chemistry, a superoxide is a compound that contains the superoxide ion, which has the chemical formula . The systematic name of the anion is dioxide(1−). The reactive oxygen ion superoxide is particularly important as the product of the one-electron reduction of dioxygen , which occurs widely in nature. Molecular oxygen (dioxygen) is a diradical containing two unpaired electrons, and superoxide results from the addition of an electron which fills one of the two degenerate molecular orbitals, leaving a charged ionic species with a single unpaired electron and a net negative charge of −1. Both dioxygen and the superoxide anion are free radicals that exhibit paramagnetism. Superoxide was historically also known as "hyperoxide". Salts Superoxide forms salts with alkali metals and alkaline earth metals. The salts sodium superoxide (), potassium superoxide (), rubidium superoxide () and caesium superoxide () are prepared by the reaction of with the respect ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
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NADPH
Nicotinamide adenine dinucleotide phosphate, abbreviated NADP or, in older notation, TPN (triphosphopyridine nucleotide), is a cofactor used in anabolic reactions, such as the Calvin cycle and lipid and nucleic acid syntheses, which require NADPH as a reducing agent ('hydrogen source'). NADPH is the reduced form, whereas NADP is the oxidized form. NADP is used by all forms of cellular life. NADP is essential for life because it is needed for cellular respiration. NADP differs from NAD by the presence of an additional phosphate group on the 2' position of the ribose ring that carries the adenine moiety. This extra phosphate is added by NAD+ kinase and removed by NADP+ phosphatase. Biosynthesis NADP In general, NADP+ is synthesized before NADPH is. Such a reaction usually starts with NAD+ from either the de-novo or the salvage pathway, with NAD+ kinase adding the extra phosphate group. ADP-ribosyl cyclase allows for synthesis from nicotinamide in the salvage pathway, ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
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Flavin Adenine Dinucleotide
In biochemistry, flavin adenine dinucleotide (FAD) is a redox-active coenzyme associated with various proteins, which is involved with several enzymatic reactions in metabolism. A flavoprotein is a protein that contains a flavin group, which may be in the form of FAD or flavin mononucleotide (FMN). Many flavoproteins are known: components of the succinate dehydrogenase complex, α-ketoglutarate dehydrogenase, and a component of the pyruvate dehydrogenase complex. FAD can exist in four redox states, which are the flavin-N(5)-oxide, quinone, semiquinone, and hydroquinone. FAD is converted between these states by accepting or donating electrons. FAD, in its fully oxidized form, or quinone form, accepts two electrons and two protons to become FADH2 (hydroquinone form). The semiquinone (FADH·) can be formed by either reduction of FAD or oxidation of FADH2 by accepting or donating one electron and one proton, respectively. Some proteins, however, generate and maintain a super ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
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Tetrahydrobiopterin
Tetrahydrobiopterin (BH4, THB), also known as sapropterin ( INN), is a cofactor of the three aromatic amino acid hydroxylase enzymes, used in the metabolism of amino acid phenylalanine and in the biosynthesis of the neurotransmitters serotonin (5-hydroxytryptamine, 5-HT), melatonin, dopamine, norepinephrine (noradrenaline), epinephrine (adrenaline), and is a cofactor for the production of nitric oxide (NO) by the nitric oxide synthases. Chemically, its structure is that of a (dihydropteridine reductase) reduced pteridine derivative (quinonoid dihydrobiopterin). Tetrahydrobiopterin is available as a tablet for oral administration in the form of sapropterin dihydrochloride (BH4*2HCL). It was approved for use in the United States as a tablet in December 2007 and as a powder in December 2013. It was approved for use in the European Union in December 2008, Canada in April 2010, and Japan in July 2008. It is sold under the brand names Kuvan and Biopten. The typical cost of treatin ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
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Heme
Heme (American English), or haem (Commonwealth English, both pronounced /Help:IPA/English, hi:m/ ), is a ring-shaped iron-containing molecule that commonly serves as a Ligand (biochemistry), ligand of various proteins, more notably as a Prosthetic group, component of hemoglobin, which is necessary to bind oxygen in the bloodstream. It is composed of four pyrrole rings with 2 Vinyl group, vinyl and 2 propionic acid side chains. Heme is biosynthesized in both the bone marrow and the liver. Heme plays a critical role in multiple different redox reactions in mammals, due to its ability to carry the oxygen molecule. Reactions include oxidative metabolism (cytochrome c oxidase, succinate dehydrogenase), xenobiotic detoxification via cytochrome P450 pathways (including Drug metabolism, metabolism of some drugs), gas sensing (Guanylate cyclase, guanyl cyclases, nitric oxide synthase), and microRNA processing (DGCR8). Heme is a coordination complex "consisting of an iron ion coordinated ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
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Dioxygen
There are several known allotropes of oxygen. The most familiar is molecular oxygen (), present at significant levels in Earth's atmosphere and also known as dioxygen or triplet oxygen. Another is the highly reactive ozone (). Others are: * Atomic oxygen (), a free radical. * Singlet oxygen (), one of two metastable states of molecular oxygen. * Tetraoxygen (), another metastable form. * Solid oxygen, existing in six variously colored phases, of which one is octaoxygen (, red oxygen) and another one metallic (ζ-oxygen). Atomic oxygen Atomic oxygen, denoted O or O1, is very reactive, as the individual atoms of oxygen tend to quickly bond with nearby molecules. Its lowest-energy electronic state is a spin triplet, designated by the term symbol 3P. On Earth's surface, it exists naturally for a very short time. In outer space, the presence of ample ultraviolet radiation results in a low Earth orbit atmosphere in which 96% of the oxygen occurs in atomic form. [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |