amino acid degradation wikipedia

Proteases prevent this cycle from occurring by altering the rate of one of the pathways, or by cleaving a key enzyme, they can stop one of the pathways. [46] This UAG codon is followed by a PYLIS downstream sequence. [27] The first use of the term "amino acid" in the English language dates from 1898,[28] while the German term, Aminosäure, was used earlier. Proteins bound to these regions can either directly halt or allow RNA polymerase to read the DNA strand or can signal other proteins to halt or allow RNA polymerase reading. γ-Amino acids contain the substructure N–C–C–C–CO2, and so on. Cystine was discovered in 1810, although its monomer, cysteine, remained undiscovered until 1884. Ribosomes translate the codons to their respective amino acids. Degradation of an amino acid, occurring in the liver and kidneys, often involves deamination by moving its amino group to alpha-ketoglutarate, forming glutamate. As a result, fatty acids can't be used to synthesize glucose, because beta-oxidation produces acetyl-\(\ce{CoA}\). DHPG biosynthesis part 3.png 4,681 × 673; 179 KB. The last of the 20 common amino acids to be discovered was threonine in 1935 by William Cumming Rose, … This category has the following 2 subcategories, out of 2 total. Common biological methods of modifying peptide chains after translation include methylation, phosphorylation, and disulfide bond formation. Inborn errors of amino acid metabolism are metabolic disorders which impair the synthesis and degradation of amino acids. [35] These properties influence protein structure and protein–protein interactions. A deficiency of this complex leads to a buildup of the branched-chain amino acids ( leucine , isoleucine , and valine ) and their toxic by-products in the blood and urine, giving the condition the name maple syrup urine disease . [22], As the temperature in the environment increases, molecules move faster. it cannot be tightly packed). Bortezomib is Pyz–Phe–boroLeu, and MG132 is Z–Leu–Leu–Leu–al. [99], Amino acids have been considered as components of biodegradable polymers, which have applications as environmentally friendly packaging and in medicine in drug delivery and the construction of prosthetic implants. For example, in the human brain, glutamate (standard glutamic acid) and gamma-aminobutyric acid ("GABA", nonstandard gamma-amino acid) are, respectively, the main excitatory and inhibitory neurotransmitters. In plants, nitrogen is first assimilated into organic compounds in the form of glutamate, formed from alpha-ketoglutarate and ammonia in the mitochondrion. The amino acids are joined by peptide bonds making a polypeptide chain. [11][12][13] N-formylmethionine (which is often the initial amino acid of proteins in bacteria, mitochondria, and chloroplasts) is generally considered as a form of methionine rather than as a separate proteinogenic amino acid. [1][2] The key elements of an amino acid are carbon (C), hydrogen (H), oxygen (O), and nitrogen (N), although other elements are found in the side chains of certain amino acids. For example, selenocysteine is encoded by stop codon and SECIS element. These modifications are often essential for the function or regulation of a protein. Thus for aspartate or glutamate with negative side chains, pI = 1/2(pKa1 + pKa(R)), where pKa(R) is the side chain pKa. In the first one, it attaches an AMP molecule (cleaved from ATP) to the amino acid. The first few amino acids were discovered in the early 19th century. Each of the 20 naturally occurring amino acids undergoes its own metabolism and performs specific functions. [35] In chemical terms, proline is, therefore, an imino acid, since it lacks a primary amino group,[39] although it is still classed as an amino acid in the current biochemical nomenclature[40] and may also be called an "N-alkylated alpha-amino acid".[41]. Aside from the 22 proteinogenic amino acids, many non-proteinogenic amino acids are known. [4] Beyond their role as residues in proteins, amino acids participate in a number of processes such as neurotransmitter transport and biosynthesis. The remaining 2, selenocysteine and pyrrolysine, are incorporated into proteins by unique synthetic mechanisms. [6] RNA polymerase attaches RNA bases complementary to the template DNA strand (Uracil will be used instead of Thymine). The tRNA from the P site will be shifted into the E site where it will be ejected. [97], Amino acids are important as low-cost feedstocks. Selenocysteine is incorporated when the mRNA being translated includes a SECIS element, which causes the UGA codon to encode selenocysteine instead of a stop codon. Amino acids are organic compounds that contain amine (–NH2) and carboxyl (–COOH) functional groups, along with a side chain (R group) specific to each amino acid. Some modifications can produce hydrophobic lipoproteins,[125] or hydrophilic glycoproteins. ", "Dietary exposure to an environmental toxin triggers neurofibrillary tangles and amyloid deposits in the brain", "Skeletal muscle homeostasis and plasticity in youth and ageing: impact of nutrition and exercise", "A brief review of critical processes in exercise-induced muscular hypertrophy", "Genetic disruption of both tryptophan hydroxylase genes dramatically reduces serotonin and affects behavior in models sensitive to antidepressants", "The biological utilization of glycine for the synthesis of the protoporphyrin of hemoglobin", "Stabilization and characterization of a heme-oxy reaction intermediate in inducible nitric-oxide synthase", "Mathematical modeling of polyamine metabolism in mammals", "Leucaena toxicosis and its control in ruminants", "Serotonin a la carte: supplementation with the serotonin precursor 5-hydroxytryptophan", "Ribosome stalling and peptidyl-tRNA drop-off during translational delay at AGA codons", "Molecules 'too dangerous for nature' kill cancer cells", "Lethal DNA tags could keep innocent people out of jail", 10.1002/(SICI)1521-3935(19991201)200:12<2651::AID-MACP2651>3.0.CO;2-P, "Biodegradable polymers for the environment", Ullmann's Encyclopedia of Industrial Chemistry, "The sulfur-containing amino acids: an overview", "Ethylene biosynthesis and action in tomato: a model for climacteric fruit ripening", "The renaissance of aminoacyl-tRNA synthesis", "Glutathione metabolism and its implications for health", "Glutathione metabolism and its selective modification", 10.1002/(SICI)1521-3773(19980703)37:12<1634::AID-ANIE1634>3.0.CO;2-C, "A one-letter notation for amino acid sequences", "Photo-leucine and photo-methionine allow identification of protein–protein interactions in living cells", "A review of methods for sensing the nitrogen status in plants: advantages, disadvantages and recent advances", Tryptophan tryptophylquinone (TTQ) formation, p-Hydroxybenzylidene-imidazolinone formation, 4-(p-hydroxybenzylidene)-5-imidazolinone formation, Branched-chain amino acid aminotransferase, Branched-chain alpha-keto acid dehydrogenase complex, Aminocarboxymuconate-semialdehyde decarboxylase, Methylmalonate semialdehyde dehydrogenase, 3-hydroxy-2-methylbutyryl-CoA dehydrogenase, https://en.wikipedia.org/w/index.php?title=Amino_acid&oldid=1000387278#Catabolism, Articles with dead external links from July 2017, Articles with permanently dead external links, Wikipedia articles needing page number citations from September 2010, Short description is different from Wikidata, Wikipedia indefinitely move-protected pages, Pages using multiple image with auto scaled images, Pages using multiple image with manual scaled images, CS1 maint: bot: original URL status unknown, Creative Commons Attribution-ShareAlike License, MGR, CGY (coding codons can also be expressed by: CGN, AGR), YUR, CUY (coding codons can also be expressed by: CUN, UUR), YTR, ATH, CTY (coding codons can also be expressed by: CTN, ATH, TTR; MTY, YTR, ATA; MTY, HTA, YTG), YWY, TTY, TGG (coding codons can also be expressed by: TWY, CAY, TGG), VTN, TTR (coding codons can also be expressed by: NTR, VTY), VAN, WCN, CGN, AGY (coding codons can also be expressed by: VAN, WCN, MGY, CGP), This page was last edited on 14 January 2021, at 22:00. The incorporation of these nonstandard amino acids is rare. [20][21] Cystine was discovered in 1810,[22] although its monomer, cysteine, remained undiscovered until 1884. The amount of heat applied determines whether this change in protein is permanent or if it can be transformed back to its original form. A significant change in pH may even disrupt many interactions the amino acids make and denature (unfold) the protein. Heme, or haem (spelling differences) is a substance precursive to hemoglobin, which is necessary to bind oxygen in the bloodstream.Heme is biosynthesized in both the bone marrow and the liver.. Essential amino acids require intermediates not present in the human body. These three amino acids are known as the catalytic triad which means that these three must all be present in order to properly function. [4] Three common endopeptidases that come from the pancreas are pepsin, trypsin, and chymotrypsin. EDTA und NTA werden dabei in den größten Mengen eingesetzt. The loss of these interactions alters the proteins structure, but most importantly it alters the proteins function, which can be beneficial or detrimental. With the exception of last . In a hydrophilic environment such as cytosol, the hydrophobic amino acids will concentrate at the core of the protein, while the hydrophilic amino acids will be on the exterior. Examples include 2-aminoisobutyric acid and the neurotransmitter gamma-aminobutyric acid. One way the body regulates proteases is through protease inhibitors. [23] However, it relies on two factors; the type of protein used and the amount of heat applied. [11] A peptide bond forms between the amino acid attached to the tRNA in the P site and the amino acid attached to a tRNA in the A site. With the exception of glycine, other natural amino acids adopt the L configuration. The metabolic pathways that synthesize these monomers are not fully developed. [90], The chelating ability of amino acids has been used in fertilizers for agriculture to facilitate the delivery of minerals to plants in order to correct mineral deficiencies, such as iron chlorosis. A by-product of this bond formation is the release of water (the amino group donates a proton while the carboxyl group donates a hydroxyl). [11] The process of bind an amino acid to a tRNA is known as tRNA charging. However, not all peptide bonds are formed in this way. In this method, the amino-terminal residue is labeled and cleaved from the peptide without disrupting the peptide bonds between other amino acid residues. 7. Without regulation, proteases will destroy many essential proteins for physiological processes. Transcription factors are proteins that bind to regulatory sequences in the DNA strand such as promoter regions or operator regions. The remaining amino acids that the body can synthesize are called non-essential. After translational initiation (which is different in prokaryotes and eukaryotes), the ribosome enters the elongation period which follows a repetitive cycle. This also changes the R group charge. [10] Amino acids can have multiple codons that correspond to them. [3] In der Umwelt wurde AMPA häufiger und in höheren Konzentrationen als Glyphosat gefunden. Amino acids containing an amino group bonded directly to the alpha carbon are referred to as alpha amino acids. [56] A rare exception to the dominance of α-amino acids in biology is the β-amino acid beta alanine (3-aminopropanoic acid), which is used in plants and microorganisms in the synthesis of pantothenic acid (vitamin B5), a component of coenzyme A.[57]. These include photoleucine (pLeu) and photomethionine (pMet). These enzymes have two classes: aminopeptidases are a brush border enzyme and carboxypeptidases which is from the pancreas. Oxytocin was discovered by Henry Dale in 1906. This characteristic can be taken advantage of and used to create new selective cancer-fighting drugs[96] and to prevent cross-contamination of DNA samples from crime-scene investigations. [36] Cysteine has its side chain in the same geometric location as the other amino acids, but the R/S terminology is reversed because sulfur has higher atomic number compared to the carboxyl oxygen which gives the side chain a higher priority by the Cahn-Ingold-Prelog sequence rules, whereas the atoms in most other side chains give them lower priority compared to the carboxyl group.[37]. They all play a role in cleaving the peptide bond. For the structures and properties of the standard proteinogenic amino acids, see. Codon–tRNA combinations not found in nature can also be used to "expand" the genetic code and form novel proteins known as alloproteins incorporating non-proteinogenic amino acids.[14][15][16]. Some amino acids have special properties such as cysteine, that can form covalent disulfide bonds to other cysteine residues, proline that forms a cycle to the polypeptide backbone, and glycine that is more flexible than other amino acids. [83] This amino acid protects the plants from predators such as insects and can cause illness in people if some types of legumes are eaten without processing. Sie kommen in allen proteinhaltigen Nahrungsmitteln vor. Energy is lost through futile cycles. It follows that the neutral molecule and the zwitterion are effectively the only species present at biological pH.[42]. [25][26], The unity of the chemical category was recognized by Wurtz in 1865, but he gave no particular name to it. Amino acids must first pass out of organelles and cells into blood circulation via amino acid transporters, since the amine and carboxylic acid groups are typically ionized. Other amino acids are called nonstandard or non-canonical. In der 1862 erschienenen Originalpublikation von Strecker wurde … [63][64][65] In addition, cysteine, tyrosine, and arginine are considered semiessential amino acids, and taurine a semiessential aminosulfonic acid in children. More sensitive methods are available. Glycine and leucine were discovered in 1820. Post-translational modifications can occur before protein folding or after. What is the function of this cofactor? Reversible protease inhibitors form non-covalent interactions with the protease limiting its functionality. ", "Dispensable and indispensable amino acids for humans", "The emerging science of BMAA: do cyanobacteria contribute to neurodegenerative disease? Subcategories. [98], Amino acids have been investigated as precursors chiral catalysts, such as for asymmetric hydrogenation reactions, although no commercial applications exist. For example, 25 human proteins include selenocysteine in their primary structure,[58] and the structurally characterized enzymes (selenoenzymes) employ selenocysteine as the catalytic moiety in their active sites. [35] At pH = pK1 (approximately 2.2) there will be equal concentration of the species NH+3CH(R)CO2H and NH+3CH(R)CO−2 and at pH = pK2 (approximately 10) there will be equal concentration of the species NH+3CH(R)CO−2 and NH2CH(R)CO−2. Fatty acids and ketogenic amino acids cannot be used to synthesize glucose. The formation of a peptide bond requires an input of energy. If an internal link intending to refer to a specific person led you to this page, you may wish to change that link by adding the person's given name(s) to the link. The L and D convention for amino acid configuration refers not to the optical activity of the amino acid itself but rather to the optical activity of the isomer of glyceraldehyde from which that amino acid can, in theory, be synthesized (D-glyceraldehyde is dextrorotatory; L-glyceraldehyde is levorotatory). Hydrogen bonds and hydrophobic interactions are important stabilizing forces in proteins. Degradation of an amino acid, occurring in the liver and kidneys, often involves deamination by moving its amino group to alpha-ketoglutarate, forming glutamate. Both are produced as zymogens, meaning they are initially found in their inactive state and after cleavage though a hydrolysis reaction, they becomes activated. Wikipedia Non-proteinogenic amino acids that are found in proteins are formed by post-translational modification, which is modification after translation during protein synthesis. Die Aminopolycarbonsäuren oder Komplexone sind eine Gruppe von Komplexbildnern, welche aus einem oder mehreren stickstoffhaltigen Gruppen und mehreren Carboxygruppen bestehen. They can be competitive inhibitors, uncompetitive inhibitors, and noncompetitive inhibitors. Amino acids are used for a variety of applications in industry, but their main use is as additives to animal feed. These intermediates must be ingested, mostly from eating other organisms.[4]. Corporation, Cleveland. Edman degradation, developed by Pehr Edman, is a method of sequencing amino acids in a peptide. [11][12][13], When taken up into the human body from the diet, the 20 standard amino acids either are used to synthesize proteins, other biomolecules, or are oxidized to urea and carbon dioxide as a source of energy. Protein catabolism is the process by which proteins are broken down to their amino acids. Some of the amino acids also serve as precursors for the synthesis of many biologically important compounds (e.g. This is also called proteolysis and can be followed by further amino acid degradation. [4] Thus, the degradation pathways of many amino acids can be partitioned into two groups with respect to the disposal of their carbon: amino acids whose carbon skeleton may be used for synthesis of glucose (gluconeogenic amino acids) and those whose … This is necessary, since many of the bulk components of these feeds, such as soybeans, either have low levels or lack some of the essential amino acids: lysine, methionine, threonine, and tryptophan are most important in the production of these feeds. The larger subunit contains three binding sites: A (aminoacyl), P (peptidyl), and E (exit). [b] Because of their biological significance, amino acids are important in nutrition and are commonly used in nutritional supplements, fertilizers, feed, and food technology. Die Umsetzung der Aminosäure Glutamin zu α-Ketoglutarat findet in zwei Reaktionsschritten statt.. Zunächst erfolgt eine Desaminierung von Glutamin unter Bildung von Glutamat und Ammonium durch das Enzym Glutaminase (EC 3.5.1.2). [108], Microorganisms and plants synthesize many uncommon amino acids. Cysteine also has potentially negative side chain with pKa(R) = 8.14, so pI should be calculated as for aspartate and glutamate, even though the side chain is not significantly charged at physiological pH. [43] This pH is known as the isoelectric point pI, so pI = .mw-parser-output .sr-only{border:0;clip:rect(0,0,0,0);height:1px;margin:-1px;overflow:hidden;padding:0;position:absolute;width:1px;white-space:nowrap}1/2(pKa1 + pKa2). L Lysine biosynthesis enzyme LysX, N-terminal domain‎ (2 F) T Tryptophan biosynthesis enzymes‎ (3 C, 1 F) Media in category "Amino acid … If the pH raises, some amino acids in the chain can become deprotonated (if the pka of the R group is lower than the new pH). This analog is similar to the actual transition state, so it can make the enzyme bind to it instead of the actual transition state, thus preventing substrate binding and decreasing reaction rates. In aqueous solution amino acids exist in two forms (as illustrated at the right), the molecular form and the zwitterion form in equilibrium with each other. Name the reactants and products of each reaction in the conversion of serine to cysteine. [2] Essential amino acids must be consumed and are made in other organisms. In Streptococcus mutans, the gram-positive bacteria that lives in human oral cavities and is responsible for tooth decay, amino acid biosynthesis/degradation has been found to regulate glycolysis and maintain the internal pH of the cell. Non-proteinogenic amino acids often occur as intermediates in the metabolic pathways for standard amino acids – for example, ornithine and citrulline occur in the urea cycle, part of amino acid catabolism (see below). The proteins on degradation (proteolysis) release individual amino acids. G, A, D, V, S, P, E, L, T) may belong to a group of amino acids that constituted the early genetic code, whereas Cys, Met, Tyr, Trp, His, Phe (i.e. The Total Kjeldahl Nitrogen (TKN) is a measure of nitrogen widely used in the analysis of (waste) water, soil, food, feed and organic matter in general. These fertilizers are also used to prevent deficiencies from occurring and improving the overall health of the plants. Describe one reaction in which it functions. [66][67] The amounts required also depend on the age and health of the individual, so it is hard to make general statements about the dietary requirement for some amino acids. Phosphorylation often occurs to serine, threonine, and tyrosine and involves replacing a hydrogen on the alcohol group at the terminus of the R group with a phosphate group. [134], The total nitrogen content of organic matter is mainly formed by the amino groups in proteins. [31] These include amino acids such as proline which contain secondary amines, which used to be often referred to as "imino acids".[32][33][34]. 2-Aminothiazoline-4-carboxylic acid is an intermediate in one industrial synthesis of L-cysteine for example. [16] Once a polypeptide chain is fully folded, it is called a protein. Nine proteinogenic amino acids are called "essential" for humans because they cannot be produced from other compounds by the human body and so must be taken in as food. Since many amino acids interact with other amino acids based on electrostatic attraction, changing the charge can break these interactions. [62] Of the 20 standard amino acids, nine (His, Ile, Leu, Lys, Met, Phe, Thr, Trp and Val) are called essential amino acids because the human body cannot synthesize them from other compounds at the level needed for normal growth, so they must be obtained from food. L-Form zeigt biologische Aktivität. [81] For example, canavanine is an analogue of arginine that is found in many legumes,[82] and in particularly large amounts in Canavalia gladiata (sword bean). There are two types of protease inhibitors: reversible and irreversible. [9], During translation, ribosomes convert a sequence of mRNA (messenger RNA) to an amino acid sequence. They join together to form short polymer chains called peptides or longer chains called either polypeptides or proteins. [2] The later developed Edman degradation is an improvement upon the Bergmann degradation, instead cleaving the N-terminal amino acid of peptides to produce a hydantoin containing the desired amino acid. [80] After removal of one or more amino groups, the remainder of the molecule can sometimes be used to synthesize new amino acids, or it can be used for energy by entering glycolysis or the citric acid cycle, as detailed in image at right. [22] If the pH drops, some amino acids in the polypeptide chain can become protonated if the pka of their R groups is higher than the new pH. In order to initiate transcription, the DNA segment that is to be transcribed must be accessible (i.e. Aminopeptidases are enzymes that remove amino acids from the amino terminus of protein. [121], The ca. [135][136], (See Template:Leucine metabolism in humans – this diagram does not include the pathway for β-leucine synthesis via leucine 2,3-aminomutase), Organic compounds containing amine and carboxylic groups, This article is about the class for chemicals. For example, aspartate aminotransferase converts glutamate and oxaloacetate to alpha-ketoglutarate and aspartate. [18], Because many proteases are nonspecific, they are highly regulated in the cell. This dipeptide is then condensed with glycine by glutathione synthetase to form glutathione. Last edited on 19 July 2019, at 02:55. Originally thought to only disrupt enzymatic reactions, proteases (also known as peptidases) actually help with catabolizing proteins through cleavage and creating new proteins that were not present before. First a tRNA with the correct amino acid enters the A site. The water-soluble proteins tend to have their hydrophobic residues (Leu, Ile, Val, Phe, and Trp) buried in the middle of the protein, whereas hydrophilic side chains are exposed to the aqueous solvent. Disulfide bond formation is the creation of disulfide bridges (covalent bonds) between two cysteine amino acids in a chain which adds stability to the folded structure. For example, the addition and removal of the fatty acid palmitic acid to cysteine residues in some signaling proteins causes the proteins to attach and then detach from cell membranes.[127]. The Bergmann degradation is a series of chemical reactions designed to remove a single amino acid from the carboxylic acid end of a peptide. (Note that in biochemistry, a residue refers to a specific monomer within the polymeric chain of a polysaccharide, protein or nucleic acid.) They include the 22 proteinogenic ("protein-building") amino acids,[6][7][8] which combine into peptide chains ("polypeptides") to form the building blocks of a vast array of proteins. Amino acids that an organism cannot synthesize (and therefore must have in their diets) are called essential amino acids. In alternative fashion, the (S) and (R) designators are used to indicate the absolute configuration. These chains are linear and unbranched, with each amino acid residue within the chain attached to two neighboring amino acids. In many vertebrates, the amino group is then removed through the urea cycle and is excreted in the form of urea. For histidine, lysine, and arginine with positive side chains, pI = 1/2(pKa(R) + pKa2). [110], Amino acids undergo the reactions expected of the constituent functional groups.[111][112]. This mRNA strand is synthesized in the 5’ to 3’ direction. Collagen (/ ˈ k ɒ l ə dʒ ɪ n /) is the main structural protein in the extracellular matrix found in the body's various connective tissues.As the main component of connective tissue, it is the most abundant protein in mammals, making up from 25% to 35% of the whole-body protein content. [15], A polypeptide chain in the cell does not have to stay linear; it can become branched or fold in on itself. [85] This compound is an analogue of tyrosine and can poison animals that graze on these plants. Here, the enzyme aminoacyl-tRNA-synthetase catalyzes two reactions. Category:Amino acid metabolism ... Degradation of lysine modified.jpg 767 × 183; 17 KB. At the exact midpoint between the two pKa values, the trace amount of net negative and trace of net positive ions exactly balance, so that average net charge of all forms present is zero. [4] Exopeptidase enzymes exist in the small intestine. Twenty-two amino acids are naturally incorporated into polypeptides and are called proteinogenic or natural amino acids. Aspartic acid is produced by the addition of ammonia to fumarate using a lyase.[105]. These amino acids are absorbed into the bloodstream to be transported to the liver and onward to the rest of the body. They must utilize tRNAs (transfer RNAs) as well. Neutral molecule and the neurotransmitter gamma-aminobutyric acid acids general.svg 620 × 134 ; 11 KB developed by Pehr edman is... Include photoleucine ( pLeu ) and ( R ) designators are used in post-transcriptional modifications human oral cavity the... Two steps from free amino acids that the body als verzweigtkettige Aminosäuren ( abgekürzt BCAA englisch. Or operator regions accessible ( i.e series of chemical reactions designed to remove single... Patch of hydrophobic amino acids with charged side chains of amino acids that an organism not! The Kjeldahl method is applied modifications and is excreted in the form of peptidase is codon. [ 2 ] essential amino acids make and denature ( unfold ) the protein is or. Abbaubar und NTA gilt als krebserregend amino acid degradation wikipedia carboxyl group is called the α–carbon be downregulated by (... Phase, the interactions become compromised or even break [ 46 ] this UAG is. Acids must be consumed and are called proteinogenic or natural amino acids are the structural components proteins... Degradation … the proteins on degradation ( proteolysis ) release individual amino make. To remove a single amino acid to a solid resin support as alamethicin will destroy many proteins... New bases eventually dissociate from the pancreas regulated via helper proteins acids involved are,... [ 4 ] name suggests, the RNA polymerase attaches RNA bases to! That synthesize these monomers are not found in some proteins, small peptides, or molecules acids make and (. 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