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(acetic acid; )
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Ãâó: ±¹¸³µ¶¼º°úÇпø µ¶¼º¹°ÁúÁ¤º¸DB : http://www.nitr.go.kr/nitr/contents/m134200/view.do |
| Mechanism of Action |
L-alanine¿¡ ´ëÇÑ Mechanism_Of_Action Á¤º¸ L-Alanine is a non-essential amino acid that occurs in high levels in its free state in plasma. It is produced from pyruvate by transamination. It is involved in sugar and acid metabolism, increases immunity, and provides energy for muscle tissue, brain, and the central nervous system. BCAAs are used as a source of energy for muscle cells. During prolonged exercise, BCAAs are released from skeletal muscles and their carbon backbones are used as fuel, while their nitrogen portion is used to form another amino acid, Alanine. Alanine is then converted to Glucose by the liver. This form of energy production is called the Alanine-Glucose cycle, and it plays a major role in maintaining the body's blood sugar balance.
L-arginine¿¡ ´ëÇÑ Mechanism_Of_Action Á¤º¸ Many of supplemental L-arginine's activities, including its possible anti-atherogenic actions, may be accounted for by its role as the precursor to nitric oxide or NO. NO is produced by all tissues of the body and plays very important roles in the cardiovascular system, immune system and nervous system. NO is formed from L-arginine via the enzyme nitric oxide synthase or synthetase (NOS), and the effects of NO are mainly mediated by 3,'5' -cyclic guanylate or cyclic GMP. NO activates the enzyme guanylate cyclase, which catalyzes the synthesis of cyclic GMP from guanosine triphosphate or GTP. Cyclic GMP is converted to guanylic acid via the enzyme cyclic GMP phosphodiesterase. NOS is a heme-containing enzyme with some sequences similar to cytochrome P-450 reductase. Several isoforms of NOS exist, two of which are constitutive and one of which is inducible by immunological stimuli. The constitutive NOS found in the vascular endothelium is designated eNOS and that present in the brain, spinal cord and peripheral nervous system is designated nNOS. The form of NOS induced by immunological or inflammatory stimuli is known as iNOS. iNOS may be expressed constitutively in select tissues such as lung epithelium. All the nitric oxide synthases use NADPH (reduced nicotinamide adenine dinucleotide phosphate) and oxygen (O2) as cosubstrates, as well as the cofactors FAD (flavin adenine dinucleotide), FMN (flavin mononucleotide), tetrahydrobiopterin and heme. Interestingly, ascorbic acid appears to enhance NOS activity by increasing intracellular tetrahydrobiopterin. eNOS and nNOS synthesize NO in response to an increased concentration of calcium ions or in some cases in response to calcium-independent stimuli, such as shear stress. In vitro studies of NOS indicate that the Km of the enzyme for L-arginine is in the micromolar range. The concentration of L-arginine in endothelial cells, as well as in other cells, and in plasma is in the millimolar range. What this means is that, under physiological conditions, NOS is saturated with its L-arginine substrate. In other words, L-arginine would not be expected to be rate-limiting for the enzyme, and it would not appear that supraphysiological levels of L-arginine which could occur with oral supplementation of the amino acid^would make any difference with regard to NO production. The reaction would appear to have reached its maximum level. However, in vivo studies have demonstrated that, under certain conditions, e.g. hypercholesterolemia, supplemental L-arginine could enhance endothelial-dependent vasodilation and NO production.
L-histidine¿¡ ´ëÇÑ Mechanism_Of_Action Á¤º¸ Since the actions of supplemental L-histidine are unclear, any postulated mechanism is entirely speculative. However, some facts are known about L-histidine and some of its metabolites, such as histamine and trans-urocanic acid, which suggest that supplemental L-histidine may one day be shown to have immunomodulatory and/or antioxidant activities. Low free histidine has been found in the serum of some rheumatoid arthritis patients. Serum concentrations of other amino acids have been found to be normal in these patients. L-histidine is an excellent chelating agent for such metals as copper, iron and zinc. Copper and iron participate in a reaction (Fenton reaction) that generates potent reactive oxygen species that could be destructive to tissues, including joints. L-histidine is the obligate precursor of histamine, which is produced via the decarboxylation of the amino acid. In experimental animals, tissue histamine levels increase as the amount of dietary L-histidine increases. It is likely that this would be the case in humans as well. Histamine is known to possess immunomodulatory and antioxidant activity. Suppressor T cells have H2 receptors, and histamine activates them. Promotion of suppressor T cell activity could be beneficial in rheumatoid arthritis. Further, histamine has been shown to down-regulate the production of reactive oxygen species in phagocytic cells, such as monocytes, by binding to the H2 receptors on these cells. Decreased reactive oxygen species production by phagocytes could play antioxidant, anti-inflammatory and immunomodulatory roles in such diseases as rheumatoid arthritis. This latter mechanism is the rationale for the use of histamine itself in several clinical trials studying histamine for the treatment of certain types of cancer and viral diseases. In these trials, down-regulation by histamine of reactive oxygen species formation appears to inhibit the suppression of natural killer (NK) cells and cytotoxic T lymphocytes, allowing these cells to be more effective in attacking cancer cells and virally infected cells.
L-isoleucine¿¡ ´ëÇÑ Mechanism_Of_Action Á¤º¸ (Applies to Valine, Leucine and Isoleucine) This group of essential amino acids are identified as the branched-chain amino acids, BCAAs. Because this arrangement of carbon atoms cannot be made by humans, these amino acids are an essential element in the diet. The catabolism of all three compounds initiates in muscle and yields NADH and FADH2 which can be utilized for ATP generation. The catabolism of all three of these amino acids uses the same enzymes in the first two steps. The first step in each case is a transamination using a single BCAA aminotransferase, with a-ketoglutarate as amine acceptor. As a result, three different a-keto acids are produced and are oxidized using a common branched-chain a-keto acid dehydrogenase, yielding the three different CoA derivatives. Subsequently the metabolic pathways diverge, producing many intermediates. The principal product from valine is propionylCoA, the glucogenic precursor of succinyl-CoA. Isoleucine catabolism terminates with production of acetylCoA and propionylCoA; thus isoleucine is both glucogenic and ketogenic. Leucine gives rise to acetylCoA and acetoacetylCoA, and is thus classified as strictly ketogenic. There are a number of genetic diseases associated with faulty catabolism of the BCAAs. The most common defect is in the branched-chain a-keto acid dehydrogenase. Since there is only one dehydrogenase enzyme for all three amino acids, all three a-keto acids accumulate and are excreted in the urine. The disease is known as Maple syrup urine disease because of the characteristic odor of the urine in afflicted individuals. Mental retardation in these cases is extensive. Unfortunately, since these are essential amino acids, they cannot be heavily restricted in the diet; ultimately, the life of afflicted individuals is short and development is abnormal The main neurological problems are due to poor formation of myelin in the CNS.
L-leucine¿¡ ´ëÇÑ Mechanism_Of_Action Á¤º¸ This group of essential amino acids are identified as the branched-chain amino acids, BCAAs. Because this arrangement of carbon atoms cannot be made by humans, these amino acids are an essential element in the diet. The catabolism of all three compounds initiates in muscle and yields NADH and FADH2 which can be utilized for ATP generation. The catabolism of all three of these amino acids uses the same enzymes in the first two steps. The first step in each case is a transamination using a single BCAA aminotransferase, with a-ketoglutarate as amine acceptor. As a result, three different a-keto acids are produced and are oxidized using a common branched-chain a-keto acid dehydrogenase, yielding the three different CoA derivatives. Subsequently the metabolic pathways diverge, producing many intermediates. The principal product from valine is propionylCoA, the glucogenic precursor of succinyl-CoA. Isoleucine catabolism terminates with production of acetylCoA and propionylCoA; thus isoleucine is both glucogenic and ketogenic. Leucine gives rise to acetylCoA and acetoacetylCoA, and is thus classified as strictly ketogenic. There are a number of genetic diseases associated with faulty catabolism of the BCAAs. The most common defect is in the branched-chain a-keto acid dehydrogenase. Since there is only one dehydrogenase enzyme for all three amino acids, all three a-keto acids accumulate and are excreted in the urine. The disease is known as Maple syrup urine disease because of the characteristic odor of the urine in afflicted individuals. Mental retardation in these cases is extensive. Unfortunately, since these are essential amino acids, they cannot be heavily restricted in the diet; ultimately, the life of afflicted individuals is short and development is abnormal The main neurological problems are due to poor formation of myelin in the CNS.
L-lysine¿¡ ´ëÇÑ Mechanism_Of_Action Á¤º¸ Proteins of the herpes simplex virus are rich in L-arginine, and tissue culture studies indicate an enhancing effect on viral replication when the amino acid ratio of L-arginine to L-lysine is high in the tissue culture media. When the ratio of L-lysine to L-arginine is high, viral replication and the cytopathogenicity of herpes simplex virus have been found to be inhibited. L-lysine may facilitate the absorption of calcium from the small intestine.
L-methionine¿¡ ´ëÇÑ Mechanism_Of_Action Á¤º¸ The mechanism of the possible anti-hepatotoxic activity of L-methionine is not entirely clear. It is thought that metabolism of high doses of acetaminophen in the liver lead to decreased levels of hepatic glutathione and increased oxidative stress. L-methionine is a precursor to L-cysteine. L-cysteine itself may have antioxidant activity. L-cysteine is also a precursor to the antioxidant glutathione. Antioxidant activity of L-methionine and metabolites of L-methionine appear to account for its possible anti-hepatotoxic activity. Recent research suggests that methionine itself has free-radical scavenging activity by virtue of its sulfur, as well as its chelating ability.
L-ornithine¿¡ ´ëÇÑ Mechanism_Of_Action Á¤º¸ L-Ornithine is metabolised to L-arginine. L-arginine stimulates the pituitary release of growth hormone. Burns or other injuries affect the state of L-arginine in tissues throughout the body. As De novo synthesis of L-arginine during these conditions is usually not sufficient for normal immune function, nor for normal protein synthesis, L-ornithine may have immunomodulatory and wound-healing activities under these conditions (by virtue of its metabolism to L-arginine).
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| Pharmacology |
L-alanine¿¡ ´ëÇÑ Pharmacology Á¤º¸ Is an important source of energy for muscle tissue, the brain and central nervous system; strengthens the immune system by producing antibodies; helps in the metabolism of sugars and organic acids.
L-arginine¿¡ ´ëÇÑ Pharmacology Á¤º¸ Studies have shown that is has improved immune responses to bacteria, viruses and tumor cells; promotes wound healing and regeneration of the liver; causes the release of growth hormones; considered crucial for optimal muscle growth and tissue repair.
L-histidine¿¡ ´ëÇÑ Pharmacology Á¤º¸ Is found abundantly in hemoglobin; has been used in the treatment of rheumatoid arthritis, allergic diseases, ulcers and anemia. A deficiency can cause poor hearing.
L-isoleucine¿¡ ´ëÇÑ Pharmacology Á¤º¸ They provide ingredients for the manufacturing of other essential biochemical components in the body, some of which are utilized for the production of energy, stimulants to the upper brain and helping you to be more alert.
L-leucine¿¡ ´ëÇÑ Pharmacology Á¤º¸ An essential amino acid. (Claim) Leucine helps with the regulation of blood-sugar levels, the growth and repair of muscle tissue (such as bones, skin and muscles), growth hormone production, wound healing as well as energy regulation. It can assist to prevent the breakdown of muscle proteins that sometimes occur after trauma or severe stress. It may also be beneficial for individuals with phenylketonuria - a condition in which the body cannot metabolize the amino acid phenylalanine
L-lysine¿¡ ´ëÇÑ Pharmacology Á¤º¸ Insures the adequate absorption of calcium; helps form collagen ( which makes up bone cartilage & connective tissues); aids in the production of antibodies, hormones & enzymes. Recent studies have shown that Lysine may be effective against herpes by improving the balance of nutrients that reduce viral growth. A deficiency may result in tiredness, inability to concentrate, irritability, bloodshot eyes, retarded growth, hair loss, anemia & reproductive problems.
L-methionine¿¡ ´ëÇÑ Pharmacology Á¤º¸ L-Methionine is a principle supplier of sulfur which prevents disorders of the hair, skin and nails; helps lower cholesterol levels by increasing the liver's production of lecithin; reduces liver fat and protects the kidneys; a natural chelating agent for heavy metals; regulates the formation of ammonia and creates ammonia-free urine which reduces bladder irritation; influences hair follicles and promotes hair growth. L-methionine may protect against the toxic effects of hepatotoxins, such as acetaminophen. Methionine may have antioxidant activity.
L-ornithine¿¡ ´ëÇÑ Pharmacology Á¤º¸ A non-essential and nonprotein amino acid, ornithine is critical for the production of the body's proteins, enzymes and muscle tissue. Ornithine plays a central role in the urea cycle and is important for the disposal of excess nitrogen (ammonia). Ornithine is the starting point for the synthesis of many polyamines such as putrescine and spermine. Ornithine supplements are claimed to enhance the release of growth hormone and to burn excess body fat. Ornithine is necessary for proper immune function and good liver function.
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| Metabolism |
L-histidine¿¡ ´ëÇÑ Metabolism Á¤º¸ # Phase_1_Metabolizing_Enzyme:Not Available
L-isoleucine¿¡ ´ëÇÑ Metabolism Á¤º¸ # Phase_1_Metabolizing_Enzyme:Not Available
L-lysine¿¡ ´ëÇÑ Metabolism Á¤º¸ # Phase_1_Metabolizing_Enzyme:Not Available
L-methionine¿¡ ´ëÇÑ Metabolism Á¤º¸ # Phase_1_Metabolizing_Enzyme:Glutamine SynthetaseMethylenetetrahydrofolate reductase
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| Absorption |
L-arginine¿¡ ´ëÇÑ Absorption Á¤º¸ Absorbed from the lumen of the small intestine into the enterocytes. Absorption is efficient and occurs by an active transport mechanism.
L-histidine¿¡ ´ëÇÑ Absorption Á¤º¸ Absorbed from the small intestine via an active transport mechanism requiring the presence of sodium.
L-isoleucine¿¡ ´ëÇÑ Absorption Á¤º¸ Absorbed from the small intestine by a sodium-dependent active-transport process
L-lysine¿¡ ´ëÇÑ Absorption Á¤º¸ Absorbed from the lumen of the small intestine into the enterocytes by an active transport process
L-methionine¿¡ ´ëÇÑ Absorption Á¤º¸ Absorbed from the lumen of the small intestine into the enterocytes by an active transport process.
L-ornithine¿¡ ´ëÇÑ Absorption Á¤º¸ Absorbed from the small intestine via a sodium-dependent active transport process
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| Pharmacokinetics |
L-glutamic acidÀÇ ¾à¹°µ¿·ÂÇÐÀÚ·á
- ºÐÆ÷ : ´ëºÎºÐÀÌ °ñ°Ý±Ù¿¡¼ ÇÕ¼ºµÇ°í ÀúÀåµÈ´Ù.
L-arginineÀÇ ¾à¹°µ¿·ÂÇÐÀÚ·á
- ÃÖ°í Ç÷Áß³óµµ µµ´Þ : °æ±¸ : 2½Ã°£
- ÃÖ´ë È¿°ú ¹ßÇö :
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- ¼ºÀåÈ£¸£¸ó º¸À¯ Áø´Ü : Á¤¸ÆÁÖ»ç : 1-2 ½Ã°£
Arginine 30 gÀ» 30ºÐ°£ Á¤¸ÆÁÖ»ç ÈÄ ¼ºÀåÈ£¸£¸óÀÇ ÃÖ´ë »ó½ÂÀÌ ¾à 1-2 ½Ã°£ ÈÄ¿¡ ³ªÅ¸³´Ù.
- ÀÛ¿ë Áö¼Ó ½Ã°£ : Á¤¸ÆÁÖ»ç : 1½Ã°£
- Èí¼ö : À§Àå°ü¿¡¼ Àß Èí¼öµÊ
- ´ë»ç : °£¿¡¼ arginase¿¡ ÀÇÇØ guanidino groupÀÌ °¡¼öºÐÇØµÇ¾î urea¿Í ornithineÀ» »ý¼ºÇÑ´Ù.
OrnithineÀº ±Ã±ØÀûÀ¸·Î glucose »ý¼º¿¡ ÀÌ¿ëµÈ´Ù.
- ¼Ò½Ç : ½ÅÀå : »ç±¸Ã¼·Î ¿©°úµÇ°í ½Å¼¼´¢°üÀ¸·Î ÀçÈí¼öµÈ´Ù.
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Aminoacetic Acid(Glycine)ÀÇ ¾à¹°µ¿·ÂÇÐÀÚ·á
- ´ë»ç : GlycineÀº ´Ü¹é, creatinine, glycocholic acid, glutathione, uric acid, heme µîÀÇ ÇÕ¼º¿¡ °ü¿©ÇÑ´Ù.
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SerineÀÌ Á¤»óÀûÀÎ ºÐÇØ»ê¹°ÀÌ´Ù.
- Ç÷Àå ¹Ý°¨±â : 85ºÐ
L-methionineÀÇ ¾à¹°µ¿·ÂÇÐÀÚ·á
- ´ë»ç : S-adenosylmethionineÀ» °ÅÃÄ homocysteineÀ¸·Î ÀüȯµÈ´Ù. ±× ÈÄ 80%°¡ cystathione, cysteine, taurine, inorganic sulphate·Î Á¡Â÷·Î ´ë»çµÈ´Ù.
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| Biotransformation |
L-arginine¿¡ ´ëÇÑ Biotransformation Á¤º¸ Some metabolism of L-arginine takes place in the enterocytes. L-arginine not metabolized in the enterocytes enters the portal circulation from whence it is transported to the liver, where again some portion of the amino acid is metabolized.
L-isoleucine¿¡ ´ëÇÑ Biotransformation Á¤º¸ Hepatic
L-lysine¿¡ ´ëÇÑ Biotransformation Á¤º¸ Hepatic
L-methionine¿¡ ´ëÇÑ Biotransformation Á¤º¸ Hepatic
L-ornithine¿¡ ´ëÇÑ Biotransformation Á¤º¸ Ornithine undergoes extensive metabolism in the liver to L-arginine, polyamines, and proline, and several other metabolites.
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| Toxicity |
L-arginine¿¡ ´ëÇÑ Toxicity Á¤º¸ Oral supplementation with L-arginine at doses up to 15 grams daily are generally well tolerated. The most common adverse reactions of higher doses from 15 to 30 grams daily are nausea, abdominal cramps and diarrhea. Some may experience these symptoms at lower doses.
L-histidine¿¡ ´ëÇÑ Toxicity Á¤º¸ ORL-RAT LD50 > 15000 mg/kg, IPR-RAT LD50 > 8000 mg/kg, ORL-MUS LD50 > 15000 mg/kg, IVN-MUS LD50 > 2000 mg/kg; Mild gastrointestinal side effects.
L-isoleucine¿¡ ´ëÇÑ Toxicity Á¤º¸ Symptoms of hypoglycemia, increased mortality in ALS patients taking large doses of BCAAs
L-lysine¿¡ ´ëÇÑ Toxicity Á¤º¸ Not Available
L-methionine¿¡ ´ëÇÑ Toxicity Á¤º¸ Doses of L-methionine of up to 250 mg daily are generally well tolerated. Higher doses may cause nausea, vomiting and headache. Healthy adults taking 8 grams of L-methionine daily for four days were found to have reduced serum folate levels and leucocytosis. Healthy adults taking 13.9 grams of L-methionine daily for five days were found to have changes in serum pH and potassium and increased urinary calcium excretion. Schizophrenic patients given 10 to 20 grams of L-methionine daily for two weeks developed functional psychoses. Single doses of 8 grams precipitated encephalopathy in patients with cirrhosis.
L-ornithine¿¡ ´ëÇÑ Toxicity Á¤º¸ Oral, rat LD50 = 10000 mg/kg
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| Drug Interactions |
L-arginine¿¡ ´ëÇÑ Drug_Interactions Á¤º¸ Not Available
L-histidine¿¡ ´ëÇÑ Drug_Interactions Á¤º¸ Not Available
L-isoleucine¿¡ ´ëÇÑ Drug_Interactions Á¤º¸ Not Available
L-lysine¿¡ ´ëÇÑ Drug_Interactions Á¤º¸ Not Available
L-methionine¿¡ ´ëÇÑ Drug_Interactions Á¤º¸ Not Available
L-ornithine¿¡ ´ëÇÑ Drug_Interactions Á¤º¸ Not Available
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CYP450 Drug Interaction |
[CYP450 TableÁ÷Á¢Á¶È¸]
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| Food Interaction |
L-methionine¿¡ ´ëÇÑ Food Interaction Á¤º¸ Take with food.
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| Drug Target |
[Drug Target]
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| Description |
L-alanine¿¡ ´ëÇÑ Description Á¤º¸ A non-essential amino acid that occurs in high levels in its free state in plasma. It is produced from pyruvate by transamination. It is involved in sugar and acid metabolism, increases immunity, and provides energy for muscle tissue, brain, and the central nervous system. [PubChem]
L-arginine¿¡ ´ëÇÑ Description Á¤º¸ An essential amino acid that is physiologically active in the L-form. [PubChem]
L-histidine¿¡ ´ëÇÑ Description Á¤º¸ An essential amino acid that is required for the production of histamine. [PubChem]
L-isoleucine¿¡ ´ëÇÑ Description Á¤º¸ An essential branched-chain aliphatic amino acid found in many proteins. It is an isomer of leucine. It is important in hemoglobin synthesis and regulation of blood sugar and energy levels. [PubChem]
L-leucine¿¡ ´ëÇÑ Description Á¤º¸ An essential branched-chain amino acid important for hemoglobin formation. [PubChem]
L-lysine¿¡ ´ëÇÑ Description Á¤º¸ L-Lysine (abbreviated as Lys or K)[1] is an α-amino acid with the chemical formula HO2CCH(NH2)(CH2)4NH2. This amino acid is an essential amino acid, which means that humans cannot synthesize it. Its codons are AAA and AAG.L-Lysine is a base, as are arginine and histidine. The ε-amino group often participates in hydrogen bonding and as a general base in catalysis. Common posttranslational modifications include methylation of the ε-amino group, giving methyl-, dimethyl-, and trimethyllysine. The latter occurs in calmodulin. Other posttranslational modifications include acetylation. Collagen contains hydroxylysine which is derived from lysine by lysyl hydroxylase. O-Glycosylation of lysine residues in the endoplasmic reticulum or Golgi apparatus is used to mark certain proteins for secretion from the cell.
L-methionine¿¡ ´ëÇÑ Description Á¤º¸ A sulfur containing essential amino acid that is important in many body functions. It is a chelating agent for heavy metals. [PubChem]
L-ornithine¿¡ ´ëÇÑ Description Á¤º¸ Ornithine is an amino acid produced in the urea cycle by the splitting off of urea from arginine. It is a central part of the urea cycle, which allows for the disposal of excess nitrogen. L-Ornithine is a precursor of citrulline and arginine.
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| Drug Category |
L-alanine¿¡ ´ëÇÑ Drug_Category Á¤º¸ Dietary supplementMicronutrientNon-Essential Amino Acids
L-arginine¿¡ ´ëÇÑ Drug_Category Á¤º¸ Conditionally Essential Amino AcidsDietary supplementMicronutrient
L-histidine¿¡ ´ëÇÑ Drug_Category Á¤º¸ Conditionally Essential Amino AcidsDietary supplementMicronutrient
L-isoleucine¿¡ ´ëÇÑ Drug_Category Á¤º¸ Dietary supplementEssential Amino AcidsMicronutrient
L-leucine¿¡ ´ëÇÑ Drug_Category Á¤º¸ Dietary supplementEssential Amino AcidsMicronutrient
L-lysine¿¡ ´ëÇÑ Drug_Category Á¤º¸ Dietary supplementEssential Amino AcidsMicronutrient
L-methionine¿¡ ´ëÇÑ Drug_Category Á¤º¸ Dietary supplementEssential Amino AcidsMicronutrient
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| Smiles String Canonical |
L-alanine¿¡ ´ëÇÑ Smiles_String_canonical Á¤º¸ CC(N)C(O)=O
L-arginine¿¡ ´ëÇÑ Smiles_String_canonical Á¤º¸ NC(CCCN=C(N)N)C(O)=O
L-histidine¿¡ ´ëÇÑ Smiles_String_canonical Á¤º¸ NC(CC1=CN=CN1)C(O)=O
L-isoleucine¿¡ ´ëÇÑ Smiles_String_canonical Á¤º¸ CCC(C)C(N)C(O)=O
L-leucine¿¡ ´ëÇÑ Smiles_String_canonical Á¤º¸ CC(C)CC(N)C(O)=O
L-lysine¿¡ ´ëÇÑ Smiles_String_canonical Á¤º¸ NCCCCC(N)C(O)=O
L-methionine¿¡ ´ëÇÑ Smiles_String_canonical Á¤º¸ CSCCC(N)C(O)=O
L-ornithine¿¡ ´ëÇÑ Smiles_String_canonical Á¤º¸ NCCCC(N)C(O)=O
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| Smiles String Isomeric |
L-alanine¿¡ ´ëÇÑ Smiles_String_isomeric Á¤º¸ C[C@H](N)C(O)=O
L-arginine¿¡ ´ëÇÑ Smiles_String_isomeric Á¤º¸ N[C@@H](CCC\N=C(\N)N)C(O)=O
L-histidine¿¡ ´ëÇÑ Smiles_String_isomeric Á¤º¸ N[C@@H](CC1=CN=CN1)C(O)=O
L-isoleucine¿¡ ´ëÇÑ Smiles_String_isomeric Á¤º¸ CC[C@H](C)[C@H](N)C(O)=O
L-leucine¿¡ ´ëÇÑ Smiles_String_isomeric Á¤º¸ CC(C)C[C@@H](N)C(O)=O
L-lysine¿¡ ´ëÇÑ Smiles_String_isomeric Á¤º¸ NCCCC[C@H](N)C(O)=O
L-methionine¿¡ ´ëÇÑ Smiles_String_isomeric Á¤º¸ CSCC[C@H](N)C(O)=O
L-ornithine¿¡ ´ëÇÑ Smiles_String_isomeric Á¤º¸ NCCC[C@H](N)C(O)=O
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| InChI Identifier |
L-alanine¿¡ ´ëÇÑ InChI_Identifier Á¤º¸ InChI=1/C3H7NO2/c1-2(4)3(5)6/h2H,4H2,1H3,(H,5,6)/t2-/m0/s1/f/h5H
L-arginine¿¡ ´ëÇÑ InChI_Identifier Á¤º¸ InChI=1/C6H14N4O2/c7-4(5(11)12)2-1-3-10-6(8)9/h4H,1-3,7H2,(H,11,12)(H4,8,9,10)/t4-/m0/s1/f/h11H,8-9H2
L-histidine¿¡ ´ëÇÑ InChI_Identifier Á¤º¸ InChI=1/C6H9N3O2/c7-5(6(10)11)1-4-2-8-3-9-4/h2-3,5H,1,7H2,(H,8,9)(H,10,11)/t5-/m0/s1/f/h9-10H
L-isoleucine¿¡ ´ëÇÑ InChI_Identifier Á¤º¸ InChI=1/C6H13NO2/c1-3-4(2)5(7)6(8)9/h4-5H,3,7H2,1-2H3,(H,8,9)/t4-,5-/m0/s1/f/h8H
L-leucine¿¡ ´ëÇÑ InChI_Identifier Á¤º¸ InChI=1/C6H13NO2/c1-4(2)3-5(7)6(8)9/h4-5H,3,7H2,1-2H3,(H,8,9)/f/h8H
L-lysine¿¡ ´ëÇÑ InChI_Identifier Á¤º¸ InChI=1/C6H14N2O2/c7-4-2-1-3-5(8)6(9)10/h5H,1-4,7-8H2,(H,9,10)/t5-/m0/s1/f/h9H
L-methionine¿¡ ´ëÇÑ InChI_Identifier Á¤º¸ InChI=1/C5H11NO2S/c1-9-3-2-4(6)5(7)8/h4H,2-3,6H2,1H3,(H,7,8)/t4-/m0/s1/f/h7H
L-ornithine¿¡ ´ëÇÑ InChI_Identifier Á¤º¸ InChI=1/C5H12N2O2/c6-3-1-2-4(7)5(8)9/h4H,1-3,6-7H2,(H,8,9)/t4-/m0/s1/f/h8H
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| Chemical IUPAC Name |
L-alanine¿¡ ´ëÇÑ Chemical_IUPAC_Name Á¤º¸ (2S)-2-aminopropanoic acid
L-arginine¿¡ ´ëÇÑ Chemical_IUPAC_Name Á¤º¸ (2S)-2-amino-5-(diaminomethylideneamino)pentanoic acid
L-histidine¿¡ ´ëÇÑ Chemical_IUPAC_Name Á¤º¸ (2S)-2-amino-3-(3H-imidazol-4-yl)propanoic acid
L-isoleucine¿¡ ´ëÇÑ Chemical_IUPAC_Name Á¤º¸ (2S,3S)-2-amino-3-methylpentanoic acid
L-leucine¿¡ ´ëÇÑ Chemical_IUPAC_Name Á¤º¸ 2-amino-4-methylpentanoic acid
L-lysine¿¡ ´ëÇÑ Chemical_IUPAC_Name Á¤º¸ (2S)-2,6-diaminohexanoic acid
L-methionine¿¡ ´ëÇÑ Chemical_IUPAC_Name Á¤º¸ (2S)-2-amino-4-methylsulfanylbutanoic acid
L-ornithine¿¡ ´ëÇÑ Chemical_IUPAC_Name Á¤º¸ (2S)-2,5-diaminopentanoic acid
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| Drug-Induced Toxicity Related Proteins |
LYSINE ÀÇ Drug-Induced Toxicity Related ProteinÁ¤º¸ Replated Protein:Tamm-Horsfall protein Drug:Lysine Toxicity:persisting acute renal failure . [¹Ù·Î°¡±â] METHIONINE ÀÇ Drug-Induced Toxicity Related ProteinÁ¤º¸ Replated Protein:NMDA receptor-regulated protein Drug:methionine Toxicity:cerebrovascular disease. [¹Ù·Î°¡±â] Replated Protein:Cystathionine beta-synthase Drug:methionine Toxicity:lipoprotein peroxidation and platelet aggregation. [¹Ù·Î°¡±â] Replated Protein:Methylenetetrahydrofolate reductase Drug:methionine Toxicity:lipoprotein peroxidation and platelet aggregation. [¹Ù·Î°¡±â]
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ÀüÈ: 02-3486-1061 ¤Ó À̸ÞÀÏ: webmaster@druginfo.co.kr
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