Chemical Formula: C6H13NO2
Chemical Formula C6H13NO2
Found 178 metabolite its formula value is C6H13NO2
L-Leucine
Leucine (Leu) or L-leucine is an alpha-amino acid. These are amino acids in which the amino group is attached to the carbon atom immediately adjacent to the carboxylate group (alpha carbon). Amino acids are organic compounds that contain amino (‚ÄìNH2) and carboxyl (‚ÄìCOOH) functional groups, along with a side chain (R group) specific to each amino acid. L-leucine is one of 20 proteinogenic amino acids, i.e., the amino acids used in the biosynthesis of proteins. Leucine is found in all organisms ranging from bacteria to plants to animals. It is classified as a non-polar, uncharged (at physiological pH) aliphatic amino acid. Leucine is essential in humans, meaning the body cannot synthesize it, and it must be obtained from the diet. Human dietary sources are foods that contain protein, such as meats, dairy products, soy products, beans and legumes. L-Leucine is a branched chain amino acid (BCAA). The BCAAs consist of leucine, valine and isoleucine (and occasionally threonine). BCAAs are essential amino acids whose carbon structure is marked by a branch point at the beta-carbon position. BCAAs are critical to human life and are particularly involved in stress, energy and muscle metabolism. BCAA supplementation as therapy, both oral and intravenous, in human health and disease holds great promise. BCAAs have different metabolic routes, with valine going solely to carbohydrates (glucogenic), leucine solely to fats (ketogenic) and isoleucine being both a glucogenic and a ketogenic amino acid. The different metabolism accounts for different requirements for these essential amino acids in humans: 12 mg/kg, 14 mg/kg and 16 mg/kg of valine, leucine and isoleucine respectively. The primary metabolic end products of leucine metabolism are acetyl-CoA and acetoacetate; consequently, it is one of the two exclusively ketogenic amino acids, with lysine being the other. Leucine is the most important ketogenic amino acid in humans. The vast majority of l-leucine metabolism is initially catalyzed by the branched-chain amino acid aminotransferase enzyme, producing alpha-ketoisocaproate (alpha-KIC). alpha-KIC is metabolized by the mitochondrial enzyme branched-chain alpha-ketoacid dehydrogenase, which converts it to isovaleryl-CoA. Isovaleryl-CoA is subsequently metabolized by the enzyme isovaleryl-CoA dehydrogenase and converted to beta-methylcrotonyl-CoA (MC-CoA), which is used in the synthesis of acetyl-CoA and other compounds. During biotin deficiency, HMB can be synthesized from MC-CoA via enoyl-CoA hydratase and an unknown thioesterase enzyme, which convert MC-CoA into HMB-CoA and HMB-CoA into HMB respectively. Leucine has the capacity to directly stimulate myofibrillar muscle protein synthesis (PMID 15051860). This effect of leucine arises results from its role as an activator of the mechanistic target of rapamycin (mTOR) (PMID 23551944) a serine-threonine protein kinase that regulates protein biosynthesis and cell growth. The activation of mTOR by leucine is mediated through Rag GTPases. Leucine, like other BCAAs, is associated with insulin resistance. In particular, higher levels of leucine are observed in the blood of diabetic mice, rats, and humans (PMID 25287287). BCAAs such as leucine have different deficiency symptoms. Valine deficiency is marked by neurological defects in the brain, while isoleucine deficiency is marked by muscle tremors. Persistently low leucine levels can result in decreased appetite, poor feeding, lethargy, poor growth, weight loss, skin rashes, hair loss, and desquamation. Many types of inborn errors of BCAA metabolism exist and these are marked by various abnormalities. The most common form is maple syrup urine disease, marked by a characteristic urinary odor. Other abnormalities are associated with a wide range of symptoms, such as mental retardation, ataxia, hypoglycemia, spinal muscle atrophy, rash, vomiting and excessive muscle movement. Most forms of BCAA metabolism errors are corrected by dietary res... L-leucine is the L-enantiomer of leucine. It has a role as a plant metabolite, an Escherichia coli metabolite, a Saccharomyces cerevisiae metabolite, a human metabolite, an algal metabolite and a mouse metabolite. It is a pyruvate family amino acid, a proteinogenic amino acid, a leucine and a L-alpha-amino acid. It is a conjugate base of a L-leucinium. It is a conjugate acid of a L-leucinate. It is an enantiomer of a D-leucine. It is a tautomer of a L-leucine zwitterion. An essential branched-chain amino acid important for hemoglobin formation. L-Leucine is a metabolite found in or produced by Escherichia coli (strain K12, MG1655). Leucine is one of nine essential amino acids in humans (provided by food), Leucine is important for protein synthesis and many metabolic functions. Leucine contributes to regulation of blood-sugar levels; growth and repair of muscle and bone tissue; growth hormone production; and wound healing. Leucine also prevents breakdown of muscle proteins after trauma or severe stress and may be beneficial for individuals with phenylketonuria. Leucine is available in many foods and deficiency is rare. (NCI04) Leucine (abbreviated as Leu or L)[2] is a branched-chain л±-amino acid with the chemical formulaHO2CCH(NH2)CH2CH(CH3)2. Leucine is classified as a hydrophobic amino acid due to its aliphatic isobutyl side chain. It is encoded by six codons (UUA, UUG, CUU, CUC, CUA, and CUG) and is a major component of the subunits in ferritin, astacin, and other buffer proteins. Leucine is an essential amino acid, meaning that the human body cannot synthesize it, and it therefore must be ingested. It is important for hemoglobin formation. An essential branched-chain amino acid important for hemoglobin formation. See also: Isoleucine; Leucine (component of) ... View More ... Dietary supplement, nutrient [DFC]. (±)-Leucine is found in many foods, some of which are green bell pepper, italian sweet red pepper, green zucchini, and red bell pepper. L-Leucine. CAS Common Chemistry. CAS, a division of the American Chemical Society, n.d. https://commonchemistry.cas.org/detail?cas_rn=61-90-5 (retrieved 2024-07-01) (CAS RN: 61-90-5). Licensed under the Attribution-Noncommercial 4.0 International License (CC BY-NC 4.0). L-Leucine is an essential branched-chain amino acid (BCAA), which activates the mTOR signaling pathway[1]. L-Leucine is an essential branched-chain amino acid (BCAA), which activates the mTOR signaling pathway[1]. L-Leucine is an essential branched-chain amino acid (BCAA), which activates the mTOR signaling pathway[1]. L-Leucine is an essential branched-chain amino acid (BCAA), which activates the mTOR signaling pathway[1].
L-Isoleucine
Isoleucine (Ile) or L-isoleucine is an alpha-amino acid. These are amino acids in which the amino group is attached to the carbon atom immediately adjacent to the carboxylate group (alpha carbon). Amino acids are organic compounds that contain amino (–NH2) and carboxyl (–COOH) functional groups, along with a side chain (R group) specific to each amino acid. L-isolecuine is one of 20 proteinogenic amino acids, i.e., the amino acids used in the biosynthesis of proteins. Isoleucine is found in all organisms ranging from bacteria to plants to animals. It is classified as a non-polar, uncharged (at physiological pH) aliphatic amino acid. Isoleucine is an essential amino acid in humans, meaning the body cannot synthesize it and that it must be obtained from the diet. In plants and microorganisms, isoleucine is synthesized starting from pyruvate and alpha-ketobutyrate. Isoleucine is classified as a branched chain amino acid (BCAA). BCAAs include three amino acids: isoleucine, leucine and valine. They are alpha amino acids whose carbon structure is marked by a beta branch point. Despite their structural similarities, BCAAs have different metabolic routes, with valine going solely to carbohydrates (glucogenic), leucine solely to fats (ketogenic) and isoleucine being both a glucogenic and a ketogenic amino acid. Isoleucine is catabolized via with alpha-ketoglutarate where upon it is oxidized and split into propionyl-CoA and acetyl-CoA. Propionyl-CoA is converted into succinyl-CoA, a TCA cycle intermediate which can be converted into oxaloacetate for gluconeogenesis (hence glucogenic). The acetyl-CoA can be fed into the TCA cycle by condensing with oxaloacetate to form citrate or used in the synthesis of ketone bodies or fatty acids. The different metabolism of BCAAs accounts for different requirements for these essential amino acids in humans: 12 mg/kg, 14 mg/kg and 16 mg/kg of valine, leucine and isoleucine are required respectively. Furthermore, these amino acids have different deficiency symptoms. Valine deficiency is marked by neurological defects in the brain, while isoleucine deficiency is marked by muscle tremors. BCAAs are decreased in patients with liver disease, such as hepatitis, hepatic coma, cirrhosis, extrahepatic biliary atresia. An inability to break down isoleucine, along with other amino acids, is associated with maple syrup urine disease (MSUD) (PMID: 34125801). Isoleucine, like other BCAAs, is associated with insulin resistance. In particular, higher levels of isoleucine are observed in the blood of diabetic mice, rats, and humans (PMID 25287287). Mice fed an isoleucine deprivation diet for one day have improved insulin sensitivity, and feeding of an isoleucine deprivation diet for one week significantly decreases blood glucose levels (PMID: 24684822). L-isoleucine is the L-enantiomer of isoleucine. It has a role as a Saccharomyces cerevisiae metabolite, an Escherichia coli metabolite, a plant metabolite, a human metabolite, an algal metabolite and a mouse metabolite. It is an aspartate family amino acid, a proteinogenic amino acid, an isoleucine and a L-alpha-amino acid. It is a conjugate base of a L-isoleucinium. It is a conjugate acid of a L-isoleucinate. It is an enantiomer of a D-isoleucine. It is a tautomer of a L-isoleucine zwitterion. 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. L-Isoleucine is a metabolite found in or produced by Escherichia coli (strain K12, MG1655). Isoleucine is one of nine essential amino acids in humans (present in dietary proteins), Isoleucine has diverse physiological functions, such as assisting wound healing, detoxification of nitrogenous wastes, stimulating immune function, and promoting secretion of several hormones. Necessary for hemoglobin formation and regulating blood sugar and energy levels, isoleucine is concentrated in muscle tissues in humans. Isoleucine is found especially in meats, fish, cheese, eggs, and most seeds and nuts. (NCI04) L-Isoleucine is one of the essential amino acids that cannot be made by the body and is known for its ability to help endurance and assist in the repair and rebuilding of muscle. This amino acid is important to body builders as it helps boost energy and helps the body recover from training. L-Isoleucine is also classified as a branched-chain amino acid (BCAA). It helps promote muscle recovery after exercise. Isoleucine is actually broken down for energy within the muscle tissue. It is important in hemoglobin synthesis and regulation of blood sugar and energy levels. 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. L-Isoleucine. CAS Common Chemistry. CAS, a division of the American Chemical Society, n.d. https://commonchemistry.cas.org/detail?cas_rn=73-32-5 (retrieved 2024-07-01) (CAS RN: 73-32-5). Licensed under the Attribution-Noncommercial 4.0 International License (CC BY-NC 4.0). L-isoleucine is a nonpolar hydrophobic amino acid[1]. L-Isoleucine is an essential amino acid. L-isoleucine is a nonpolar hydrophobic amino acid[1]. L-Isoleucine is an essential amino acid.
Aminocaproic acid
Aminocaproic acid (marketed as Amicar) is a drug used to treat bleeding disorders. It is an antifibrinolytic agent that acts by inhibiting plasminogen activators which have fibrinolytic properties. It is a derivative of the amino acid lysine. It binds reversibly to the kringle domain of plasminogen and blocks the binding of plasminogen to fibrin and its activation to plasmin. [HMDB] Aminocaproic acid (marketed as Amicar) is a drug used to treat bleeding disorders. It is an antifibrinolytic agent that acts by inhibiting plasminogen activators which have fibrinolytic properties. It is a derivative of the amino acid lysine. It binds reversibly to the kringle domain of plasminogen and blocks the binding of plasminogen to fibrin and its activation to plasmin. B - Blood and blood forming organs > B02 - Antihemorrhagics > B02A - Antifibrinolytics > B02AA - Amino acids Acquisition and generation of the data is financially supported in part by CREST/JST. D006401 - Hematologic Agents > D003029 - Coagulants > D006490 - Hemostatics C78275 - Agent Affecting Blood or Body Fluid > C78311 - Hemostatic Agent D050299 - Fibrin Modulating Agents > D000933 - Antifibrinolytic Agents IPB_RECORD: 266; CONFIDENCE confident structure KEIO_ID A053 6-Aminocaproic acid (EACA), a monoamino carboxylic acid, is a potent and orally active inhibitor of plasmin and plasminogen. 6-Aminocaproic acid is a potent antifibrinolytic agent. 6-Aminocaproic acid prevents clot lysis through the competitive binding of lysine residues on plasminogen, inhibiting plasmin formation and reducing fibrinolysis. 6-Aminocaproic acid can be used for the research of bleeding disorders[1][2].
L-Norleucine
L-Norleucine, also known as L-aminohexanoate or caprine, belongs to the class of organic compounds known as l-alpha-amino acids. These are alpha amino acids which have the L-configuration of the alpha-carbon atom. Thus, L-norleucine is considered to be a fatty acid lipid molecule. An unnatural amino acid that is used experimentally to study protein structure and function. L-Norleucine is a very hydrophobic molecule, practically insoluble in water, and relatively neutral. L-Norleucine exists in all eukaryotes, ranging from yeast to humans. Outside of the human body, L-Norleucine has been detected, but not quantified in cow milk. This could make L-norleucine a potential biomarker for the consumption of these foods. It binds reversibly to the kringle domain of plasminogen and blocks the binding of plasminogen to fibrin and its activation to plasmin. An unnatural amino acid that is used experimentally to study protein structure and function. It is structurally similar to methionine, however it does not contain sulfur. Acquisition and generation of the data is financially supported in part by CREST/JST. CONFIDENCE standard compound; INTERNAL_ID 22 KEIO_ID N014 L-Norleucine ((S)-2-Aminohexanoic acid) is an isomer of leucine, specifically affects protein synthesis in skeletal muscle, and has antivirus activity.
Beta-Leucine
Beta-leucine is a metabolite that is in the middle of a controversy over its presence in the human body. While there are reports that claim it as a human metabolite, there are others that deny its existence. Two examples:. Circulating levels of beta-leucine are elevated in the cobalamin-deficient state of pernicious anemia. Levels of leucine, on the other hand, are much lower. It is proposed that leucine 2,3-aminomutase, the cobalamin-dependent enzyme that catalyzes the interconversion of leucine and beta-leucine, is the affected enzyme in pernicious anemia and causes these results by preventing the synthesis of leucine from beta-leucine. The synthesis of leucine by human leukocytes and hair roots and by rat liver extracts has been shown to occur when either branched chain fatty acids or valine metabolites are the substances. The synthesis is dependent upon adenosylcobalamin and is inhibited by intrinsic factor (PMID:7430116). Using forms of beta-leucine and leucine that contain several deuterium atoms in place of several hydrogen atoms as internal standards, techniques have been developed which make it possible to detect and quantitate as little as 0.1 mumol/liter of beta-leucine or leucine in human serum and in incubations containing rat liver supernatant. beta-Leucine was not detectable, i.e. less than 0.1 mumol/liter, in any sera from 50 normal human subjects or in any sera from 50 cobalamin-deficient patients. Experiments in which beta-leucine, leucine, isostearic acid, or isocaproic acid were incubated with rat liver supernatant in the presence or absence of adenosylcobalamin or cobalamin-binding protein failed to demonstrate the formation of leucine or beta-leucine or their interconversion under any of the conditions studied. We conclude that beta-leucine is not present in human blood and that the existence of leucine 2,3-aminomutase in mammalian tissues remains to be established (PMID 3356699). Beta-leucine is found to be associated with cobalamin deficiency, which is an inborn error of metabolism. Beta-leucine is a metabolite that is in the middle of a controversy over its presence in the human body. While there are reports that claim it as a human metabolite, there are others that deny its existence. Two examples: Acquisition and generation of the data is financially supported in part by CREST/JST. KEIO_ID L057 3-Amino-4-methylpentanoic acid is a beta amino acid and positional isomer of L-leucine which is naturally produced in humans via the metabolism of L-leucine by the enzyme leucine 2,3-aminomutase.
N,N-Diethylglycine
An N-alkyl glycine that is glycine in which the amino group is replaced by a diethylnitrilo group.
D-Leucine
An essential branched-chain amino acid important for hemoglobin formation. [PubChem]; Branched chain amino acids (BCAA) are essential amino acids whose carbon structure is marked by a branch point. These three amino acids are critical to human life and are particularly involved in stress, energy and muscle metabolism. BCAA supplementation as therapy, both oral and intravenous, in human health and disease holds great promise. BCAA denotes valine, isoleucine and leucine which are branched chain essential amino acids. Despite their structural similarities, the branched amino acids have different metabolic routes, with valine going solely to carbohydrates, leucine solely to fats and isoleucine to both. The different metabolism accounts for different requirements for these essential amino acids in humans: 12 mg/kg, 14 mg/kg and 16 mg/kg of valine, leucine and isoleucine respectively. Furthermore, these amino acids have different deficiency symptoms. Valine deficiency is marked by neurological defects in the brain, while isoleucine deficiency is marked by muscle tremors. Many types of inborn errors of BCAA metabolism exist, and are marked by various abnormalities. The most common form is the maple syrup urine disease, marked by a characteristic urinary odor. Other abnormalities are associated with a wide range of symptoms, such as mental retardation, ataxia, hypoglycemia, spinal muscle atrophy, rash, vomiting and excessive muscle movement. Most forms of BCAA metabolism errors are corrected by dietary restriction of BCAA and at least one form is correctable by supplementation with 10 mg of biotin daily. BCAA are useful because they are metabolized primarily by muscle. Stress state- e.g surgery, trauma, cirrhosis, infections, fever and starvation--require proportionately more BCAA than other amino acids and probably proportionately more leucine than either valine or isoleucine. BCAA and other amino acids are frequently fed intravenously (TPN) to malnourished surgical patients and in some cases of severe trauma. BCAA, particularly leucine, stimulate protein synthesis, increase reutilization of amino acids in many organs and reduce protein breakdown. Furthermore, leucine can be an important source of calories, and is superior as fuel to the ubiquitous intravenous glucose (dextrose). Leucine also stimulates insulin release, which in turn stimulates protein synthesis and inhibits protein breakdown. These effects are particularly useful in athletic training. BCAA should also replace the use of steroids as commonly used by weightlifters. Huntingtons chorea and anorexic disorders both are characterized by low serum BCAA. These diseases, as well as forms of Parkinsons, may respond to BCAA therapy. BCAA, and particularly leucine, are among the amino acids most essential for muscle health. (http://www.dcnutrition.com); Leucine (abbreviated as Leu or L) is a branched-chain amino acid with the chemical formula HO2CCH(NH2)CH2CH(CH3)2. Leucine is classified as a hydrophobic amino acid due to its aliphatic isobutyl side chain. It is encoded by six codons (UUA, UUG, CUU, CUC, CUA, and CUG) and is a major component of the subunits in ferritin, astacin and other buffer proteins. Leucine is an essential amino acid. Leucine is a branched-chain amino acid (BCAA) since it possesses an aliphatic side-chain that is non-linear. D-Leucine is a more potent anti-seizure agent than L-leucine. D-leucine potently terminates seizures even after the onset of seizure activity. D-leucine, but not L-leucine, reduces long-term potentiation but had no effect on basal synaptic transmission in vitro[1]. D-Leucine is a more potent anti-seizure agent than L-leucine. D-leucine potently terminates seizures even after the onset of seizure activity. D-leucine, but not L-leucine, reduces long-term potentiation but had no effect on basal synaptic transmission in vitro[1].
(±)-erythro-Isoleucine
(±)-erythro-Isoleucine is a flavouring ingredient, dietary supplement, and a nutrient. Branched-chain amino acids (BCAA) are essential amino acids whose carbon structure is marked by a branch point. These three amino acids are critical to human life and are particularly involved in stress, energy and muscle metabolism. BCAA supplementation as therapy, both oral and intravenous, in human health and disease holds great promise. BCAA denotes valine, isoleucine, and leucine which are branched chain essential amino acids. Despite their structural similarities, the branched amino acids have different metabolic routes, with valine going solely to carbohydrates, leucine solely to fats, and isoleucine to both. The different metabolism accounts for different requirements for these essential amino acids in humans: 12 mg/kg, 14 mg/kg, and 16 mg/kg of valine, leucine, and isoleucine respectively. Furthermore, these amino acids have different deficiency symptoms. Valine deficiency is marked by neurological defects in the brain, while isoleucine deficiency is marked by muscle tremors. BCAA are decreased in patients with liver disease such as hepatitis, hepatic coma, cirrhosis, extrahepatic biliary atresia, or portacaval shunt. Aromatic amino acids (AAA)-tyrosine, tryptophan, and phenylalanine (as well as methionine) are increased in these conditions. Valine, in particular, has been established as a useful supplemental therapy to the ailing liver. All the BCAA probably compete with AAA for absorption into the brain. Supplemental BCAA with vitamin B6 and zinc help normalize the BCAA:AAA ratio. The BCAA are not without side effects. Leucine alone, for example, exacerbates pellagra and can cause psychosis in pellagra patients by increasing excretion of niacin in the urine. Leucine may lower brain serotonin and dopamine. The ratio of leucine to other BCAA is greatest in pork, where leucine is 7 to 8 g and the other BCAA together are only 3 to 4 g (http://www.dcnutrition.com).
L-Alloisoleucine
An optically active form of alloisoleucine having L-(2S,3R)-configuration. L-Alloisoleucine is a branched chain amino acid and is a stereo-isomer of L-isoleucine. L-Alloisoleucine is a common constituent of human plasma (albeit at low levels).
D-Isoleucine
The D-enantiomer of isoleucine. Acquisition and generation of the data is financially supported in part by CREST/JST.
Leucine
A branched-chain amino acid that consists of glycine in which one of the hydrogens attached to the alpha-carbon is substituted by an isobutyl group. Leucine (symbol Leu or L)[3] is an essential amino acid that is used in the biosynthesis of proteins. Leucine is an α-amino acid, meaning it contains an α-amino group (which is in the protonated −NH3+ form under biological conditions), an α-carboxylic acid group (which is in the deprotonated −COO− form under biological conditions), and a side chain isobutyl group, making it a non-polar aliphatic amino acid. It is essential in humans, meaning the body cannot synthesize it: it must be obtained from the diet. Human dietary sources are foods that contain protein, such as meats, dairy products, soy products, and beans and other legumes. It is encoded by the codons UUA, UUG, CUU, CUC, CUA, and CUG. Leucine is named after the Greek word for "white": λευκός (leukós, "white"), after its common appearance as a white powder, a property it shares with many other amino acids.[4] Like valine and isoleucine, leucine is a branched-chain amino acid. The primary metabolic end products of leucine metabolism are acetyl-CoA and acetoacetate; consequently, it is one of the two exclusively ketogenic amino acids, with lysine being the other.[5] It is the most important ketogenic amino acid in humans.[6] Leucine and β-hydroxy β-methylbutyric acid, a minor leucine metabolite, exhibit pharmacological activity in humans and have been demonstrated to promote protein biosynthesis via the phosphorylation of the mechanistic target of rapamycin (mTOR).[7][8] L-Leucine is an essential branched-chain amino acid (BCAA), which activates the mTOR signaling pathway[1]. L-Leucine is an essential branched-chain amino acid (BCAA), which activates the mTOR signaling pathway[1]. L-Leucine is an essential branched-chain amino acid (BCAA), which activates the mTOR signaling pathway[1]. L-Leucine is an essential branched-chain amino acid (BCAA), which activates the mTOR signaling pathway[1].
N-methylvaline
N-methylvaline, also known as MeVal, D-Valine, or N-Methyl-L-valine, is an N-methylamino acid that is the N-methyl derivative of valine. It functions as a bronsted acid, a molecular entity capable of donating a hydron to an acceptor (Bronsted base) via oxoacid
6-Deoxyfagomine
6-Deoxyfagomine is an alkaloid from the roots of Lycium chinense (Chinese boxthorn). Alkaloid from the roots of Lycium chinense (Chinese boxthorn)
L-Alloisoleucine
L-alloisoleucine is a branched chain amino acid and is a stereo-isomer of L-isoleucine. It is a common constituent of human plasma (albeit at low levels). L-alloisoleucine is produced as a byproduct of isoleucine transamination. L-Isoleucine is one of the four common amino acids (the 3 others being threonine, hydroxyproline, and hydroxylysine) that have two asymmetric carbon atoms which produce four structural possibilities for the same chemical composition. L-alloisoleucine differs from L-isoleucine by having having different stereochemistry around its beta carbon. Plasma L-alloisoleucine, which is derived from L-isoleucine in vivo, can be used for the diagnosis of maple syrup urine disease (MSUD), a genetic disorder. Indeed, plasma L-alloisoleucine levels above 5 umol/L is the most specific and most sensitive diagnostic marker for all forms of MSUD (PMID: 10508118). In MSUD the degradation of the essential branched-chain L-amino acids leucine, valine, and isoleucine and their derived 2-oxoacids is impaired because of an inherited deficiency in branched-chain 2-oxoacid dehydrogenase complex (EC 1.2.4.4) activity. The accumulation of branched-chain compounds in blood and other body fluids can exert neurotoxic effects. L-alloisoleucine is a branched chain amino acid and is a stereo-isomer of L-isoleucine. It is a common constituent of human plasma (albeit at low levels). L-alloisoleucine is produced as a byproduct of isoleucine transamination. L-Isoleucine is one of the four common amino acids (the 3 others being threonine, hydroxyproline, and hydroxylysine) that have two asymmetric carbon atoms which produce four structural possibilities for the same chemical composition. L-alloisoleucine differs from L-isoleucine by having having different stereochemistry around its beta carbon. Plasma L-alloisoleucine, which is derived from L-isoleucine in vivo, can be used for the diagnosis of maple syrup urine disease (MSUD). Indeed, plasma L-alloisoleucine levels above 5 umol/L is the most specific and most sensitive diagnostic marker for all forms of MSUD (PMID: 10508118). In MSUD the degradation of the essential branched-chain L-amino acids leucine, valine, and isoleucine and their derived 2-oxoacids is impaired because of an inherited deficiency in branched-chain 2-oxoacid dehydrogenase complex (EC 1.2.4.4) activity. The accumulation of branched-chain compounds in blood and other body fluids can exert neurotoxic effects. [HMDB] L-Alloisoleucine is a branched chain amino acid and is a stereo-isomer of L-isoleucine. L-Alloisoleucine is a common constituent of human plasma (albeit at low levels).
N-(2-Hydroxyethyl)-morpholine
N-(2-Hydroxyethyl)-morpholine is a metabolite of mycophenolate mofetil. Mycophenolate mofetil (MMF) (brand names CellCept, Myfortic) is an immunosuppressant and prodrug of mycophenolic acid, used extensively in transplant medicine. It is a reversible inhibitor of inosine monophosphate dehydrogenase (IMPDH) in purine biosynthesis which is necessary for the growth of T cells and B cells. Other cells are able to recover purines via a separate, scavenger, pathway and are, thus, able to escape the effect. MMF is a less toxic alternative to azathioprine. (Wikipedia)
3-Amino-4-methylpentanoic acid
3-Amino-4-methylpentanoic acid is a beta amino acid and positional isomer of L-leucine which is naturally produced in humans via the metabolism of L-leucine by the enzyme leucine 2,3-aminomutase.
beta-alanine betaine
beta-alanine betaine, also known as beta-homobetaine or propiobetaine, is a member of the class of compounds known as tetraalkylammonium salts. Tetraalkylammonium salts are organonitrogen compounds containing a quaternary ammonium substituted with four alkyl chains. beta-alanine betaine is practically insoluble (in water) and a weakly acidic compound (based on its pKa). beta-alanine betaine can be found in a number of food items such as cabbage, ohelo berry, olive, and common salsify, which makes beta-alanine betaine a potential biomarker for the consumption of these food products.
Leucine
COVID info from PDB, Protein Data Bank Corona-virus Coronavirus SARS-CoV-2 COVID-19 SARS-CoV COVID19 SARS2 SARS L-Leucine is an essential branched-chain amino acid (BCAA), which activates the mTOR signaling pathway[1]. L-Leucine is an essential branched-chain amino acid (BCAA), which activates the mTOR signaling pathway[1]. L-Leucine is an essential branched-chain amino acid (BCAA), which activates the mTOR signaling pathway[1]. L-Leucine is an essential branched-chain amino acid (BCAA), which activates the mTOR signaling pathway[1].
Isoleucine
COVID info from PDB, Protein Data Bank Corona-virus Coronavirus SARS-CoV-2 COVID-19 SARS-CoV COVID19 SARS2 SARS L-isoleucine is a nonpolar hydrophobic amino acid[1]. L-Isoleucine is an essential amino acid. L-isoleucine is a nonpolar hydrophobic amino acid[1]. L-Isoleucine is an essential amino acid.
trimethylalanine
A beta-alanine derivative arising from quaternisation of the nitrogen of beta-alanine with three methyl groups and removal of the proton attached to the carboxy group. It is an osmoprotective compound accumulated by most members of the highly stress-tolerant Plumbaginaceae family. β-alanine betaine, also known as beta-homobetaine or propiobetaine, is a member of the class of compounds known as tetraalkylammonium salts. Tetraalkylammonium salts are organonitrogen compounds containing a quaternary ammonium substituted with four alkyl chains. β-alanine betaine is practically insoluble (in water) and a weakly acidic compound (based on its pKa). β-alanine betaine can be found in a number of food items such as cabbage, ohelo berry, olive, and common salsify, which makes β-alanine betaine a potential biomarker for the consumption of these food products.
Isoleucine
A 2-amino-3-methylpentanoic acid having either (2R,3R)- or (2S,3S)-configuration. A branched chain amino acid that consists of 3-methylpentanoic acid bearing an amino substituent at position 2. CONFIDENCE standard compound; INTERNAL_ID 5153 Acquisition and generation of the data is financially supported by the Max-Planck-Society L-isoleucine is a nonpolar hydrophobic amino acid[1]. L-Isoleucine is an essential amino acid. L-isoleucine is a nonpolar hydrophobic amino acid[1]. L-Isoleucine is an essential amino acid.
DL-Leucine
relative retention time with respect to 9-anthracene Carboxylic Acid is 0.062 relative retention time with respect to 9-anthracene Carboxylic Acid is 0.057 relative retention time with respect to 9-anthracene Carboxylic Acid is 0.055
L-Isoleucine
MS2 deconvoluted using MS2Dec from all ion fragmentation data, MetaboLights identifier MTBLS1040; AGPKZVBTJJNPAG-WHFBIAKZSA-N_STSL_0101_Isoleucine_8000fmol_180425_S2_LC02_MS02_58; Spectrum acquired as described in Naz et al 2017 PMID 28641411. Preparation and submission to MassBank of North America by Chaleckis R. and Tada I. MS2 deconvoluted using CorrDec from all ion fragmentation data, MetaboLights identifier MTBLS1040; Spectrum acquired as described in Naz et al 2017 PMID 28641411. Preparation and submission to MassBank of North America by Chaleckis R. and Tada I. CONFIDENCE standard compound; INTERNAL_ID 8 COVID info from PDB, Protein Data Bank Corona-virus Coronavirus SARS-CoV-2 COVID-19 SARS-CoV COVID19 SARS2 SARS L-isoleucine is a nonpolar hydrophobic amino acid[1]. L-Isoleucine is an essential amino acid. L-isoleucine is a nonpolar hydrophobic amino acid[1]. L-Isoleucine is an essential amino acid.
Norleucine
L-Norleucine ((S)-2-Aminohexanoic acid) is an isomer of leucine, specifically affects protein synthesis in skeletal muscle, and has antivirus activity.
L-Leucine
Flavouring ingredient; dietary supplement, nutrient. L-Leucine is found in many foods, some of which are lettuce, common bean, pacific herring, and kefir. MS2 deconvoluted using MS2Dec from all ion fragmentation data, MetaboLights identifier MTBLS1040; ROHFNLRQFUQHCH-YFKPBYRVSA-N_STSL_0102_Leucine_8000fmol_180425_S2_LC02_MS02_19; Spectrum acquired as described in Naz et al 2017 PMID 28641411. Preparation and submission to MassBank of North America by Chaleckis R. and Tada I. MS2 deconvoluted using CorrDec from all ion fragmentation data, MetaboLights identifier MTBLS1040; Spectrum acquired as described in Naz et al 2017 PMID 28641411. Preparation and submission to MassBank of North America by Chaleckis R. and Tada I. L-Leucine is an essential branched-chain amino acid (BCAA), which activates the mTOR signaling pathway[1]. L-Leucine is an essential branched-chain amino acid (BCAA), which activates the mTOR signaling pathway[1]. L-Leucine is an essential branched-chain amino acid (BCAA), which activates the mTOR signaling pathway[1]. L-Leucine is an essential branched-chain amino acid (BCAA), which activates the mTOR signaling pathway[1].
L-Norleucine
A non-proteinogenic L-alpha-amino acid comprising hexanoic acid carrying an amino group at C-2. It does not occur naturally. L-Norleucine ((S)-2-Aminohexanoic acid) is an isomer of leucine, specifically affects protein synthesis in skeletal muscle, and has antivirus activity.
6-Aminocaproic acid
6-Aminocaproic acid (EACA), a monoamino carboxylic acid, is a potent and orally active inhibitor of plasmin and plasminogen. 6-Aminocaproic acid is a potent antifibrinolytic agent. 6-Aminocaproic acid prevents clot lysis through the competitive binding of lysine residues on plasminogen, inhibiting plasmin formation and reducing fibrinolysis. 6-Aminocaproic acid can be used for the research of bleeding disorders[1][2].
L-allo-Isoleucine
L-Alloisoleucine is a branched chain amino acid and is a stereo-isomer of L-isoleucine. L-Alloisoleucine is a common constituent of human plasma (albeit at low levels).
e-Aminocaproic acid
6-Aminocaproic acid (EACA), a monoamino carboxylic acid, is a potent and orally active inhibitor of plasmin and plasminogen. 6-Aminocaproic acid is a potent antifibrinolytic agent. 6-Aminocaproic acid prevents clot lysis through the competitive binding of lysine residues on plasminogen, inhibiting plasmin formation and reducing fibrinolysis. 6-Aminocaproic acid can be used for the research of bleeding disorders[1][2].
Aminocaproic acid
B - Blood and blood forming organs > B02 - Antihemorrhagics > B02A - Antifibrinolytics > B02AA - Amino acids D006401 - Hematologic Agents > D003029 - Coagulants > D006490 - Hemostatics C78275 - Agent Affecting Blood or Body Fluid > C78311 - Hemostatic Agent D050299 - Fibrin Modulating Agents > D000933 - Antifibrinolytic Agents 6-Aminocaproic acid (EACA), a monoamino carboxylic acid, is a potent and orally active inhibitor of plasmin and plasminogen. 6-Aminocaproic acid is a potent antifibrinolytic agent. 6-Aminocaproic acid prevents clot lysis through the competitive binding of lysine residues on plasminogen, inhibiting plasmin formation and reducing fibrinolysis. 6-Aminocaproic acid can be used for the research of bleeding disorders[1][2].
Beta-Leucine
A beta-amino acid that is pentanoic acid substituted at positions 3 and 4 by amino and methyl groups respectively. 3-Amino-4-methylpentanoic acid is a beta amino acid and positional isomer of L-leucine which is naturally produced in humans via the metabolism of L-leucine by the enzyme leucine 2,3-aminomutase.
DL-Norleucine
MS2 deconvoluted using MS2Dec from all ion fragmentation data, MetaboLights identifier MTBLS1040; LRQKBLKVPFOOQJ-UHFFFAOYSA-N_STSL_0189_Norleucine_8000fmol_180831_S2_L02M02_35; Spectrum acquired as described in Naz et al 2017 PMID 28641411. Preparation and submission to MassBank of North America by Chaleckis R. and Tada I. MS2 deconvoluted using CorrDec from all ion fragmentation data, MetaboLights identifier MTBLS1040; Spectrum acquired as described in Naz et al 2017 PMID 28641411. Preparation and submission to MassBank of North America by Chaleckis R. and Tada I.
Alanine betaine
MS2 deconvoluted using MS2Dec from all ion fragmentation data, MetaboLights identifier MTBLS1040; CJKONRHMUGBAQI-UHFFFAOYSA-N_STSL_0044_alanine betaine_0125fmol_180407_S2_LC02_MS02_24; Spectrum acquired as described in Naz et al 2017 PMID 28641411. Preparation and submission to MassBank of North America by Chaleckis R. and Tada I. MS2 deconvoluted using CorrDec from all ion fragmentation data, MetaboLights identifier MTBLS1040; Spectrum acquired as described in Naz et al 2017 PMID 28641411. Preparation and submission to MassBank of North America by Chaleckis R. and Tada I.
2-Amino-4-methylpentanoic acid
Isolated from Cape gooseberry Physalis peruviana. Butyl (R)-3-hydroxybutyrate [arabinosyl-(1->6)-glucoside] is found in fruits.
Allo-isoleucine
L-Alloisoleucine is a branched chain amino acid and is a stereo-isomer of L-isoleucine. L-Alloisoleucine is a common constituent of human plasma (albeit at low levels).
N-METHYL-L-VALINE
An optically active form of N-methylvaline having L-configuration.
1-nitrohexane
A primary nitroalkane that is hexane substituted by a nitro group at position 1.
D-leucine zwitterion
A D-alpha-amino acid zwitterion arising from the transfer of a proton from the carboxy to the amino group of D-leucine; major species at pH 7.3.
D-Leucine
The D-enantiomer of leucine. D-Leucine is a more potent anti-seizure agent than L-leucine. D-leucine potently terminates seizures even after the onset of seizure activity. D-leucine, but not L-leucine, reduces long-term potentiation but had no effect on basal synaptic transmission in vitro[1]. D-Leucine is a more potent anti-seizure agent than L-leucine. D-leucine potently terminates seizures even after the onset of seizure activity. D-leucine, but not L-leucine, reduces long-term potentiation but had no effect on basal synaptic transmission in vitro[1].
L-isoleucine zwitterion
An L-alpha-amino acid zwitterion obtained by transfer of a proton from the carboxy to the amino group of L-isoleucine; major species at pH 7.3.
L-alloisoleucine zwitterion
An amino acid zwitterion resulting from a transfer of a proton from the carboxy group to the amino group of L-alloisoleucine; major species at pH 7.3.
2-Aminohexanoic acid
An alpha-amino acid that is caproic acid substituted by an amino group at position 2.
tert-butylglycine
A glycine derivative that is glycine with a tertiary butyl group at position 2.
L-2-aminohexanoic acid zwitterion
An L-alpha-amino acid zwitterion obtained from L-2-aminohexanoic acid by transfer of a proton from the carboxy group to the amino group. It is the major species at pH 7.3.
6-aminohexanoic acid zwitterion
Zwitterionic form of 6-aminohexanoic acid arising from migration of a proton from the carboxy group to the amino group; major species at pH 7.3.
6-Aminohexanoic acid
An epsilon-amino acid comprising hexanoic acid carrying an amino substituent at position C-6. Used to control postoperative bleeding, and to treat overdose effects of the thrombolytic agents streptokinase and tissue plasminogen activator.