NCBI Taxonomy: 5296

L-Tyrosine

C9H11NO3 (181.0738896)

Tyrosine (Tyr) or L-tyrosine 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-tyrosine is one of 20 proteinogenic amino acids, i.e., the amino acids used in the biosynthesis of proteins. Tyrosine is found in all organisms ranging from bacteria to plants to animals. It is classified as a non-polar, uncharged (at physiological pH) aromatic amino acid. Tyrosine is a non-essential amino acid, meaning the body can synthesize it – usually from phenylalanine. The conversion of phenylalanine to tyrosine is catalyzed by the enzyme phenylalanine hydroxylase, a monooxygenase. This enzyme catalyzes the reaction causing the addition of a hydroxyl group to the end of the 6-carbon aromatic ring of phenylalanine, such that it becomes tyrosine. Tyrosine is found in many high-protein food products such as chicken, turkey, fish, milk, yogurt, cottage cheese, cheese, peanuts, almonds, pumpkin seeds, sesame seeds, soy products, lima beans, avocados and bananas. Tyrosine is one of the few amino acids that readily passes the blood-brain barrier. Once in the brain, it is a precursor for the neurotransmitters dopamine, norepinephrine and epinephrine, better known as adrenalin. These neurotransmitters are an important part of the bodys sympathetic nervous system, and their concentrations in the body and brain are directly dependent upon dietary tyrosine. Tyrosine is not found in large concentrations throughout the body, probably because it is rapidly metabolized. Folic acid, copper and vitamin C are cofactor nutrients of these reactions. Tyrosine is also the precursor for hormones, including thyroid hormones (diiodotyrosine), catecholestrogens and the major human pigment, melanin. Tyrosine is an important amino acid in many proteins, peptides and even enkephalins, the bodys natural pain reliever. Valine and other branched amino acids, and possibly tryptophan and phenylalanine may reduce tyrosine absorption. A number of genetic errors of tyrosine metabolism have been identified, such as hawkinsinuria and tyrosinemia I. The most common feature of these diseases is the increased amount of tyrosine in the blood, which is marked by decreased motor activity, lethargy and poor feeding. Infection and intellectual deficits may occur. Vitamin C supplements can help reverse these disease symptoms. Some adults also develop elevated tyrosine in their blood. This typically indicates a need for more vitamin C. More tyrosine is needed under stress, and tyrosine supplements prevent the stress-induced depletion of norepinephrine and can help aleviate biochemical depression. However, tyrosine may not be good for treating psychosis. Many antipsychotic medications apparently function by inhibiting tyrosine metabolism. L-Dopa, which is directly used in Parkinsons, is made from tyrosine. Tyrosine, the nutrient, can be used as an adjunct in the treatment of Parkinsons. Peripheral metabolism of tyrosine necessitates large doses of tyrosine, however, compared to L-Dopa (http://www.dcnutrition.com). In addition to its role as a precursor for neurotransmitters, tyrosine plays an important role for the function of many proteins. Within many proteins or enzymes, certain tyrosine residues can be tagged (at the hydroxyl group) with a phosphate group (phosphorylated) by specialized protein kinases. In its phosphorylated form, tyrosine is called phosphotyrosine. Tyrosine phosphorylation is considered to be one of the key steps in signal transduction and regulation of enzymatic activity. Tyrosine (or its precursor phenylalanine) is also needed to synthesize the benzoquinone structure which forms part of coenzyme Q10. L-tyrosine is an optically active form of tyrosine having L-configuration. It has a role as an EC 1.3.1.43 (arogenate dehydrogenase) inhibitor, a nutraceutical, a micronutrient and a fundamental metabolite. It is an erythrose 4-phosphate/phosphoenolpyruvate family amino acid, a proteinogenic amino acid, a tyrosine and a L-alpha-amino acid. It is functionally related to a L-tyrosinal. It is a conjugate base of a L-tyrosinium. It is a conjugate acid of a L-tyrosinate(1-). It is an enantiomer of a D-tyrosine. It is a tautomer of a L-tyrosine zwitterion. Tyrosine is a non-essential amino acid. In animals it is synthesized from [phenylalanine]. It is also the precursor of [epinephrine], thyroid hormones, and melanin. L-Tyrosine is a metabolite found in or produced by Escherichia coli (strain K12, MG1655). L-Tyrosine is the levorotatory isomer of the aromatic amino acid tyrosine. L-tyrosine is a naturally occurring tyrosine and is synthesized in vivo from L-phenylalanine. It is considered a non-essential amino acid; however, in patients with phenylketonuria who lack phenylalanine hydroxylase and cannot convert phenylalanine into tyrosine, it is considered an essential nutrient. In vivo, tyrosine plays a role in protein synthesis and serves as a precursor for the synthesis of catecholamines, thyroxine, and melanin. Tyrosine is an essential amino acid that readily passes the blood-brain barrier. Once in the brain, it is a precursor for the neurotransmitters dopamine, norepinephrine and epinephrine, better known as adrenalin. These neurotransmitters are an important part of the bodys sympathetic nervous system, and their concentrations in the body and brain are directly dependent upon dietary tyrosine. Tyrosine is not found in large concentrations throughout the body, probably because it is rapidly metabolized. Folic acid, copper and vitamin C are cofactor nutrients of these reactions. Tyrosine is also the precursor for hormones, thyroid, catecholestrogens and the major human pigment, melanin. Tyrosine is an important amino acid in many proteins, peptides and even enkephalins, the bodys natural pain reliever. Valine and other branched amino acids, and possibly tryptophan and phenylalanine may reduce tyrosine absorption. A number of genetic errors of tyrosine metabolism occur. Most common is the increased amount of tyrosine in the blood of premature infants, which is marked by decreased motor activity, lethargy and poor feeding. Infection and intellectual deficits may occur. Vitamin C supplements reverse the disease. Some adults also develop elevated tyrosine in their blood. This indicates a need for more vitamin C. More tyrosine is needed under stress, and tyrosine supplements prevent the stress-induced depletion of norepinephrine and can cure biochemical depression. However, tyrosine may not be good for psychosis. Many antipsychotic medications apparently function by inhibiting tyrosine metabolism. L-dopa, which is directly used in Parkinsons, is made from tyrosine. Tyrosine, the nutrient, can be used as an adjunct in the treatment of Parkinsons. Peripheral metabolism of tyrosine necessitates large doses of tyrosine, however, compared to L-dopa. A non-essential amino acid. In animals it is synthesized from PHENYLALANINE. It is also the precursor of EPINEPHRINE; THYROID HORMONES; and melanin. Dietary supplement, nutrient. Flavouring ingredient. L-Tyrosine is found in many foods, some of which are blue crab, sweet rowanberry, lemon sole, and alpine sweetvetch. An optically active form of tyrosine having L-configuration. L-Tyrosine. CAS Common Chemistry. CAS, a division of the American Chemical Society, n.d. https://commonchemistry.cas.org/detail?cas_rn=60-18-4 (retrieved 2024-07-01) (CAS RN: 60-18-4). Licensed under the Attribution-Noncommercial 4.0 International License (CC BY-NC 4.0). L-Tyrosine is a non-essential amino acid which can inhibit citrate synthase activity in the posterior cortex. L-Tyrosine is a non-essential amino acid which can inhibit citrate synthase activity in the posterior cortex.

L-Leucine

C6H13NO2 (131.0946238)

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

C6H13NO2 (131.0946238)

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.

serin

C3H7NO3 (105.0425912)

Serine is an alpha-amino acid that is alanine substituted at position 3 by a hydroxy group. It has a role as a fundamental metabolite. It is an alpha-amino acid and a polar amino acid. It contains a hydroxymethyl group. It is a conjugate base of a serinium. It is a conjugate acid of a serinate. It is a tautomer of a serine zwitterion. DL-Serine, a fundamental metabolite, is a mixture of D-Serine and L-Serine. DL-Serine has antiviral activity against the multiplication of tobacco mosaic virus (TMV)[1]. DL-Serine, a fundamental metabolite, is a mixture of D-Serine and L-Serine. DL-Serine has antiviral activity against the multiplication of tobacco mosaic virus (TMV)[1]. D-Serine ((R)-Serine), an endogenous amino acid involved in glia-synapse interactions that has unique neurotransmitter characteristics, is a potent co-agonist at the NMDA glutamate receptor. D-Serinee has a cardinal modulatory role in major NMDAR-dependent processes including NMDAR-mediated neurotransmission, neurotoxicity, synaptic plasticity, and cell migration[1][2]. D-Serine ((R)-Serine), an endogenous amino acid involved in glia-synapse interactions that has unique neurotransmitter characteristics, is a potent co-agonist at the NMDA glutamate receptor. D-Serinee has a cardinal modulatory role in major NMDAR-dependent processes including NMDAR-mediated neurotransmission, neurotoxicity, synaptic plasticity, and cell migration[1][2]. L-Serine ((-)-Serine; (S)-Serine), one of the so-called non-essential amino acids, plays a central role in cellular proliferation. L-Serine ((-)-Serine; (S)-Serine), one of the so-called non-essential amino acids, plays a central role in cellular proliferation.

L-Arginine

C6H14N4O2 (174.1116704)

Arginine (Arg), also known as L-argninine, 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. 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-asparagine is one of 20 proteinogenic amino acids, i.e., the amino acids used in the biosynthesis of proteins. Arginine is found in all organisms ranging from bacteria to plants to animals. Arginine is an essential amino acid that is physiologically active in the L-form. It is classified as a charged, basic, aliphatic amino acid. Arginine is considered to be a basic amino acid as it has a strongly basic guanidinium group. With a pKa of 12.48, the guanidinium group is positively charged in neutral, acidic, and even most basic environments. Because of the conjugation between the double bond and the nitrogen lone pairs, the positive charge is delocalized. This group is able to form multiple H-bonds. In mammals, arginine is formally classified as a semi-essential or conditionally essential amino acid, depending on the developmental stage and health status of the individual. Infants are unable to effectively synthesize arginine, making it nutritionally essential for infants. Adults, however, are able to synthesize arginine in the urea cycle. L-Arginine is an amino acid that has numerous functions in the body. It helps dispose of ammonia, is used to make compounds such as nitric oxide, creatine, L-glutamate, and L-proline, and it can be converted into glucose and glycogen if needed. Arginine also plays an important role in cell division, immunity and wound healing. Arginine is the immediate precursor of nitric oxide (NO), an important signaling molecule which can act as a second messenger, as well as an intercellular messenger which regulates vasodilation, and also has functions in the immune systems reaction to infection. Nitric oxide is made via the enzyme nitric oxide synthase (PMID 10690324). Arginine is also a precursor for several important nitrogen-containing compounds including urea, ornithine, and agmatine. Arginine is necessary for the synthesis of creatine and can be used for the synthesis of polyamines (mainly through ornithine and to a lesser degree through agmatine, citrulline, and glutamate.) The presence of asymmetric dimethylarginine (ADMA) in serum or plasma, a close relative of argninine, inhibits the nitric oxide synthase reaction. ADMA is considered a marker for vascular disease, just as L-arginine is considered a sign of a healthy endothelium. In large doses, L-arginine also stimulates the release of the hormones growth hormone and prolactin. Arginine is a known inducer of mTOR (mammalian target of rapamycin) and is responsible for inducing protein synthesis through the mTOR pathway. mTOR inhibition by rapamycin partially reduces arginine-induced protein synthesis (PMID: 20841502). Catabolic disease states such as sepsis, injury, and cancer cause an increase in arginine utilization, which can exceed normal body production, leading to arginine depletion. Arginine also activates AMP kinase (AMPK) which then stimulates skeletal muscle fatty acid oxidation and muscle glucose uptake, thereby increasing insulin secretion by pancreatic beta-cells (PMID: 21311355). Arginine is found in plant and animal proteins, such as dairy products, meat, poultry, fish, and nuts. The ratio of L-arginine to lysine is also important: soy and other plant proteins have more L-arginine than animal sources of protein. [Spectral] L-Arginine (exact mass = 174.11168) and L-Histidine (exact mass = 155.06948) were not completely separated on HPLC under the present analytical conditions as described in AC$XXX. Additionally some of the peaks in this data contains dimers and other unidentified ions. L-Arginine. CAS Common Chemistry. CAS, a division of the American Chemical Society, n.d. https://commonchemistry.cas.org/detail?cas_rn=74-79-3 (retrieved 2024-06-29) (CAS RN: 74-79-3). Licensed under the Attribution-Noncommercial 4.0 International License (CC BY-NC 4.0). L-Arginine ((S)-(+)-Arginine) is the substrate for the endothelial nitric oxide synthase (eNOS) to generate NO. L-Arginine is transported into vascular smooth muscle cells by the cationic amino acid transporter family of proteins where it is metabolized to nitric oxide (NO), polyamines, or L-proline[1][2]. L-Arginine ((S)-(+)-Arginine) is the substrate for the endothelial nitric oxide synthase (eNOS) to generate NO. L-Arginine is transported into vascular smooth muscle cells by the cationic amino acid transporter family of proteins where it is metabolized to nitric oxide (NO), polyamines, or L-proline[1][2].

L-Aspartic acid

C4H7NO4 (133.0375062)

Aspartic acid (Asp), also known as L-aspartic acid or as aspartate, the name of its anion, 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-aspartic acid is one of 20 proteinogenic amino acids, i.e., the amino acids used in the biosynthesis of proteins. Aspartic acid is found in all organisms ranging from bacteria to plants to animals. It is classified as an acidic, charged (at physiological pH), aliphatic amino acid. In humans, aspartic acid is a nonessential amino acid derived from glutamic acid by enzymes using vitamin B6. However, in the human body, aspartate is most frequently synthesized through the transamination of oxaloacetate. A non-essential amino acid is an amino acid that can be synthesized from central metabolic pathway intermediates in humans and is not required in the diet. As its name indicates, aspartic acid is the carboxylic acid analog of asparagine. The D-isomer of aspartic acid (D-aspartic acid) is one of two D-amino acids commonly found in mammals. Aspartic acid was first discovered in 1827 by Auguste-Arthur Plisson and Étienne Ossian Henry by hydrolysis of asparagine, which had been isolated from asparagus juice in 1806. Aspartate has many biochemical roles. It is a neurotransmitter, a metabolite in the urea cycle and it participates in gluconeogenesis. It carries reducing equivalents in the malate-aspartate shuttle, which utilizes the ready interconversion of aspartate and oxaloacetate, which is the oxidized (dehydrogenated) derivative of malic acid. Aspartate donates one nitrogen atom in the biosynthesis of inosine, the precursor to the purine bases which are key to DNA biosynthesis. In addition, aspartic acid acts as a hydrogen acceptor in a chain of ATP synthase. Aspartic acid is a major excitatory neurotransmitter, which is sometimes found to be increased in epileptic and stroke patients. It is decreased in depressed patients and in patients with brain atrophy. As a neurotransmitter, aspartic acid may provide resistance to fatigue and thus lead to endurance, although the evidence to support this idea is not strong (Wikipedia). Aspartic acid supplements are being evaluated. Five grams can raise blood levels. Magnesium and zinc may be natural inhibitors of some of the actions of aspartic acid. Aspartic acid, when chemically coupled with the amino acid D-phenylalanine, is a part of a natural sweetener, aspartame. This sweetener is an advance in artificial sweeteners, and is probably safe in normal doses to all except phenylketonurics. Aspartic acid may be a significant immunostimulant of the thymus and can protect against some of the damaging effects of radiation. Aspartic acid is found in higher abundance in: oysters, luncheon meats, sausage meat, wild game, sprouting seeds, oat flakes, avocado, asparagus, young sugarcane, and molasses from sugar beets. [Spectral] L-Aspartate (exact mass = 133.03751) and Taurine (exact mass = 125.01466) and L-Asparagine (exact mass = 132.05349) were not completely separated on HPLC under the present analytical conditions as described in AC$XXX. Additionally some of the peaks in this data contains dimers and other unidentified ions. [Spectral] L-Aspartate (exact mass = 133.03751) and L-Threonine (exact mass = 119.05824) were not completely separated on HPLC under the present analytical conditions as described in AC$XXX. Additionally some of the peaks in this data contains dimers and other unidentified ions. L-Aspartic acid is is an amino acid, shown to be a suitable proagent for colon-specific agent deliverly. L-Aspartic acid is is an amino acid, shown to be a suitable proagent for colon-specific agent deliverly.

L-Histidine

C6H9N3O2 (155.0694734)

Histidine (His), also known as L-histidine, 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. Histidine is one of 20 proteinogenic amino acids, i.e., the amino acids used in the biosynthesis of proteins. Histidine is found in all organisms ranging from bacteria to plants to animals. It is classified as an aliphatic, positively charged or basic amino acid. Histidine is a unique amino acid with an imidazole functional group. The acid-base properties of the imidazole side chain are relevant to the catalytic mechanism of many enzymes such as proteases. In catalytic triads, the basic nitrogen of histidine abstracts a proton from serine, threonine, or cysteine to activate it as a nucleophile. In a histidine proton shuttle, histidine is used to quickly shuttle protons. It can do this by abstracting a proton with its basic nitrogen to make a positively charged intermediate and then use another molecule to extract the proton from its acidic nitrogen. Histidine forms complexes with many metal ions. The imidazole sidechain of the histidine residue commonly serves as a ligand in metalloproteins. Histidine was first isolated by German physician Albrecht Kossel in 1896. Histidine is an essential amino acid in humans and other mammals. It was initially thought that it was only essential for infants, but longer-term studies established that it is also essential for adults. Infants four to six months old require 33 mg/kg of histidine. It is not clear how adults make small amounts of histidine, and dietary sources probably account for most of the histidine in the body. Histidine is a precursor for histamine and carnosine biosynthesis. Inborn errors of histidine metabolism, including histidinemia, maple syrup urine disease, propionic acidemia, and tyrosinemia I, exist and are marked by increased histidine levels in the blood. Elevated blood histidine is accompanied by a wide range of symptoms, from mental and physical retardation to poor intellectual functioning, emotional instability, tremor, ataxia and psychosis. Histidine and other imidazole compounds have anti-oxidant, anti-inflammatory and anti-secretory properties (PMID: 9605177 ). The efficacy of L-histidine in protecting inflamed tissue is attributed to the capacity of the imidazole ring to scavenge reactive oxygen species (ROS) generated by cells during acute inflammatory response (PMID: 9605177 ). Histidine, when administered in therapeutic quantities is able to inhibit cytokines and growth factors involved in cell and tissue damage (US patent 6150392). Histidine in medical therapies has its most promising trials in rheumatoid arthritis where up to 4.5 g daily have been used effectively in severely affected patients. Arthritis patients have been found to have low serum histidine levels, apparently because of very rapid removal of histidine from their blood (PMID: 1079527 ). Other patients besides arthritis patients that have been found to be low in serum histidine are those with chronic renal failure. Urinary levels of histidine are reduced in pediatric patients with pneumonia (PMID: 2084459 ). Asthma patients exhibit increased serum levels of histidine over normal controls (PMID: 23517038 ). Serum histidine levels are lower and are negatively associated with inflammation and oxidative stress in obese women (PMID: 23361591 ). Histidine supplementation has been shown to reduce insulin resistance, reduce BMI and fat mass and suppress inflammation and oxidative stress in obese women with metabolic syndrome. Histidine appears to suppress pro-inflammatory cytokine expression, possibly via the NF-κB pathway, in adipocytes (PMID: 23361591 ). Low plasma concentrations of histidine are associated with protein-energy... [Spectral] L-Histidine (exact mass = 155.06948) and L-Lysine (exact mass = 146.10553) and L-Arginine (exact mass = 174.11168) were not completely separated on HPLC under the present analytical conditions as described in AC$XXX. Additionally some of the peaks in this data contains dimers and other unidentified ions. [Spectral] L-Histidine (exact mass = 155.06948) and L-Arginine (exact mass = 174.11168) were not completely separated on HPLC under the present analytical conditions as described in AC$XXX. Additionally some of the peaks in this data contains dimers and other unidentified ions. Acquisition and generation of the data is financially supported in part by CREST/JST. Flavouring ingredient; dietary supplement, nutrient L-Histidine. CAS Common Chemistry. CAS, a division of the American Chemical Society, n.d. https://commonchemistry.cas.org/detail?cas_rn=71-00-1 (retrieved 2024-07-01) (CAS RN: 71-00-1). Licensed under the Attribution-Noncommercial 4.0 International License (CC BY-NC 4.0). L-Histidine is an essential amino acid for infants. L-Histidine is an inhibitor of mitochondrial glutamine transport. L-Histidine is an essential amino acid for infants. L-Histidine is an inhibitor of mitochondrial glutamine transport. L-Histidine is an essential amino acid for infants. L-Histidine is an inhibitor of mitochondrial glutamine transport.

L-Serine

C3H7NO3 (105.0425912)

Serine (Ser) or L-serine 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-serine is one of 20 proteinogenic amino acids, i.e., the amino acids used in the biosynthesis of proteins. Serine is found in all organisms ranging from bacteria to plants to animals. It is classified as a polar, uncharged (at physiological pH), aliphatic amino acid. In humans, serine is a nonessential amino acid that can be easily derived from glycine. A non-essential amino acid is an amino acid that can be synthesized from central metabolic pathway intermediates in humans and is not required in the diet. Like all the amino acid building blocks of protein and peptides, serine can become essential under certain conditions, and is thus important in maintaining health and preventing disease. L-Serine may be derived from four possible sources: dietary intake; biosynthesis from the glycolytic intermediate 3-phosphoglycerate; from glycine; and by protein and phospholipid degradation. Little data is available on the relative contributions of each of these four sources of l-serine to serine homoeostasis. It is very likely that the predominant source of l-serine will be very different in different tissues and during different stages of human development. In the biosynthetic pathway, the glycolytic intermediate 3-phosphoglycerate is converted into phosphohydroxypyruvate, in a reaction catalyzed by 3-phosphoglycerate dehydrogenase (3- PGDH; EC 1.1.1.95). Phosphohydroxypyruvate is metabolized to phosphoserine by phosphohydroxypyruvate aminotransferase (EC 2.6.1.52) and, finally, phosphoserine is converted into l-serine by phosphoserine phosphatase (PSP; EC 3.1.3.3). In liver tissue, the serine biosynthetic pathway is regulated in response to dietary and hormonal changes. Of the three synthetic enzymes, the properties of 3-PGDH and PSP are the best documented. Hormonal factors such as glucagon and corticosteroids also influence 3-PGDH and PSP activities in interactions dependent upon the diet. L-serine is the predominant source of one-carbon groups for the de novo synthesis of purine nucleotides and deoxythymidine monophosphate. It has long been recognized that, in cell cultures, L-serine is a conditional essential amino acid, because it cannot be synthesized in sufficient quantities to meet the cellular demands for its utilization. In recent years, L-serine and the products of its metabolism have been recognized not only to be essential for cell proliferation, but also to be necessary for specific functions in the central nervous system. The findings of altered levels of serine and glycine in patients with psychiatric disorders and the severe neurological abnormalities in patients with defects of L-serine synthesis underscore the importance of L-serine in brain development and function. (PMID 12534373). [Spectral] L-Serine (exact mass = 105.04259) and D-2-Aminobutyrate (exact mass = 103.06333) and 4-Aminobutanoate (exact mass = 103.06333) were not completely separated on HPLC under the present analytical conditions as described in AC$XXX. Additionally some of the peaks in this data contains dimers and other unidentified ions. Dietary supplement. L-Serine is found in many foods, some of which are cold cut, mammee apple, coho salmon, and carrot. L-Serine. CAS Common Chemistry. CAS, a division of the American Chemical Society, n.d. https://commonchemistry.cas.org/detail?cas_rn=56-45-1 (retrieved 2024-07-01) (CAS RN: 56-45-1). Licensed under the Attribution-Noncommercial 4.0 International License (CC BY-NC 4.0). L-Serine ((-)-Serine; (S)-Serine), one of the so-called non-essential amino acids, plays a central role in cellular proliferation. L-Serine ((-)-Serine; (S)-Serine), one of the so-called non-essential amino acids, plays a central role in cellular proliferation.

L-Lysine

C6H14N2O2 (146.1055224)

Lysine (Lys), also known as L-lysine 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. Lysine is one of 20 proteinogenic amino acids, i.e., the amino acids used in the biosynthesis of proteins. Lysine is found in all organisms ranging from bacteria to plants to animals. It is classified as an aliphatic, positively charged or basic amino acid. In humans, lysine is an essential amino acid, meaning the body cannot synthesize it, and it must be obtained from the diet. Lysine is high in foods such as wheat germ, cottage cheese and chicken. Of meat products, wild game and pork have the highest concentration of lysine. Fruits and vegetables contain little lysine, except avocados. Normal requirements for lysine have been found to be about 8 g per day or 12 mg/kg in adults. Children and infants need more, 44 mg/kg per day for an eleven to-twelve-year old, and 97 mg/kg per day for three-to six-month old. In organisms that synthesise lysine, it has two main biosynthetic pathways, the diaminopimelate and α-aminoadipate pathways, which employ distinct enzymes and substrates and are found in diverse organisms. Lysine catabolism occurs through one of several pathways, the most common of which is the saccharopine pathway. Lysine plays several roles in humans, most importantly proteinogenesis, but also in the crosslinking of collagen polypeptides, uptake of essential mineral nutrients, and in the production of carnitine, which is key in fatty acid metabolism. Lysine is also often involved in histone modifications, and thus, impacts the epigenome. Lysine is highly concentrated in muscle compared to most other amino acids. Normal lysine metabolism is dependent upon many nutrients including niacin, vitamin B6, riboflavin, vitamin C, glutamic acid and iron. Excess arginine antagonizes lysine. Several inborn errors of lysine metabolism are known, such as cystinuria, hyperdibasic aminoaciduria I, lysinuric protein intolerance, propionic acidemia, and tyrosinemia I. Most are marked by mental retardation with occasional diverse symptoms such as absence of secondary sex characteristics, undescended testes, abnormal facial structure, anemia, obesity, enlarged liver and spleen, and eye muscle imbalance. Lysine also may be a useful adjunct in the treatment of osteoporosis. Although high protein diets result in loss of large amounts of calcium in urine, so does lysine deficiency. Lysine may be an adjunct therapy because it reduces calcium losses in urine. Lysine deficiency also may result in immunodeficiency. Requirements for lysine are probably increased by stress. Lysine toxicity has not occurred with oral doses in humans. Lysine dosages are presently too small and may fail to reach the concentrations necessary to prove potential therapeutic applications. Lysine metabolites, amino caproic acid and carnitine have already shown their therapeutic potential. Thirty grams daily of amino caproic acid has been used as an initial daily dose in treating blood clotting disorders, indicating that the proper doses of lysine, its precursor, have yet to be used in medicine. Low lysine levels have been found in patients with Parkinsons, hypothyroidism, kidney disease, asthma and depression. The exact significance of these levels is unclear, yet lysine therapy can normalize the level and has been associated with improvement of some patients with these conditions. Abnormally elevated hydroxylysines have been found in virtually all chronic degenerative diseases and those treated with coumadin therapy. The levels of this stress marker may be improved by high doses of vitamin C. Lysine is particularly useful in therapy for marasmus (wasting) (http://www.dcnutrition.com). Lysine has also been sh... [Spectral] L-Lysine (exact mass = 146.10553) and Carnosine (exact mass = 226.10659) were not completely separated on HPLC under the present analytical conditions as described in AC$XXX. Additionally some of the peaks in this data contains dimers and other unidentified ions. Dietary supplement, nutrient. Found widely in protein hydrolysates, e.g. casein, egg albumen, fibrin, gelatin, beet molasses. Flavouring agent for a variety of foods L-Lysine. CAS Common Chemistry. CAS, a division of the American Chemical Society, n.d. https://commonchemistry.cas.org/detail?cas_rn=56-87-1 (retrieved 2024-07-01) (CAS RN: 56-87-1). Licensed under the Attribution-Noncommercial 4.0 International License (CC BY-NC 4.0). L-lysine is an essential amino acid[1][2] with important roles in connective tissues and carnitine synthesis, energy production, growth in children, and maintenance of immune functions[2]. L-lysine is an essential amino acid[1][2] with important roles in connective tissues and carnitine synthesis, energy production, growth in children, and maintenance of immune functions[2].

L-Methionine

C5H11NO2S (149.0510466)

Methionine (Met), also known as L-methionine, 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. Methionine is one of 20 proteinogenic amino acids, i.e., the amino acids used in the biosynthesis of proteins. Methionine is found in all organisms ranging from bacteria to plants to animals. It is classified as an aliphatic, non-polar amino acid. Methionine is an essential amino acid (there are 9 essential amino acids), meaning the body cannot synthesize it, and it must be obtained from the diet. It is required for normal growth and development of humans, other mammals, and avian species. In addition to being a substrate for protein synthesis, methionine is an intermediate in transmethylation reactions, serving as the major methyl group donor in vivo, including the methyl groups for DNA and RNA intermediates. Methionine is a methyl acceptor for 5-methyltetrahydrofolate-homocysteine methyltransferase (methionine synthase), the only reaction that allows for the recycling of this form of folate, and is also a methyl acceptor for the catabolism of betaine. Methionine is the metabolic precursor for cysteine. Only the sulfur atom from methionine is transferred to cysteine; the carbon skeleton of cysteine is donated by serine (PMID: 16702340 ). There is a general consensus concerning normal sulfur amino acid (SAA) requirements. WHO recommendations amount to 13 mg/kg per 24 h in healthy adults. This amount is roughly doubled in artificial nutrition regimens. In disease or after trauma, requirements may be altered for methionine, cysteine, and taurine. Although in specific cases of congenital enzyme deficiency, prematurity, or diminished liver function, hypermethioninemia or hyperhomocysteinemia may occur, SAA supplementation can be considered safe in amounts exceeding 2-3 times the minimum recommended daily intake. Apart from some very specific indications (e.g. acetaminophen poisoning) the usefulness of SAA supplementation is not yet established (PMID: 16702341 ). Methionine is known to exacerbate psychopathological symptoms in schizophrenic patients, but there is no evidence of similar effects in healthy subjects. The role of methionine as a precursor of homocysteine is the most notable cause for concern. Acute doses of methionine can lead to acute increases in plasma homocysteine, which can be used as an index of the susceptibility to cardiovascular disease. Sufficiently high doses of methionine can actually result in death. Longer-term studies in adults have indicated no adverse consequences of moderate fluctuations in dietary methionine intake, but intakes higher than 5 times the normal amount resulted in elevated homocysteine levels. These effects of methionine on homocysteine and vascular function are moderated by supplements of vitamins B-6, B-12, C, and folic acid (PMID: 16702346 ). When present in sufficiently high levels, methionine can act as an atherogen and a metabotoxin. An atherogen is a compound that when present at chronically high levels causes atherosclerosis and cardiovascular disease. A metabotoxin is an endogenously produced metabolite that causes adverse health effects at chronically high levels. Chronically high levels of methionine are associated with at least ten inborn errors of metabolism, including cystathionine beta-synthase deficiency, glycine N-methyltransferase deficiency, homocystinuria, tyrosinemia, galactosemia, homocystinuria-megaloblastic anemia due to defects in cobalamin metabolism, methionine adenosyltransferase deficiency, methylenetetrahydrofolate reductase deficiency, and S-adenosylhomocysteine (SAH) hydrolase deficiency. Chronically elevated levels of methionine in infants can lead to intellectual disability and othe... [Spectral] L-Methionine (exact mass = 149.05105) and Adenosine (exact mass = 267.09675) and S-Adenosyl-L-homocysteine (exact mass = 384.12159) were not completely separated on HPLC under the present analytical conditions as described in AC$XXX. Additionally some of the peaks in this data contains dimers and other unidentified ions. [Spectral] L-Methionine (exact mass = 149.05105) and Tyramine (exact mass = 137.08406) were not completely separated on HPLC under the present analytical conditions as described in AC$XXX. Additionally some of the peaks in this data contains dimers and other unidentified ions. l-Methionine. CAS Common Chemistry. CAS, a division of the American Chemical Society, n.d. https://commonchemistry.cas.org/detail?cas_rn=63-68-3 (retrieved 2024-07-01) (CAS RN: 63-68-3). Licensed under the Attribution-Noncommercial 4.0 International License (CC BY-NC 4.0). L-Methionine is the L-isomer of Methionine, an essential amino acid for human development. Methionine acts as a hepatoprotectant. L-Methionine is the L-isomer of Methionine, an essential amino acid for human development. Methionine acts as a hepatoprotectant.

Cysteic acid

C3H7NO5S (169.00449319999998)

Cysteic acid is a crystalline amino acid formed in the oxidation of cysteine; it is a precursor of taurine. A crystalline amino acid formed in the oxidation of cysteine; it is a precursor of taurine. [HMDB]

L-Allothreonine

C4H9NO3 (119.0582404)

L-allothreonine is the L-enantiomer of allothreonine. It has a role as an Escherichia coli metabolite and a Saccharomyces cerevisiae metabolite. It is an enantiomer of a D-allothreonine. It is a tautomer of a L-allothreonine zwitterion. Allothreonine is the substrate of the enzyme Serine hydroxymethyltransferase1 (SHMT, EC 2.1.2.1), a human cytoplasmic mRNA binding protein. SHMT uses pyridoxal 5-phosphate (PLP) and tetrahydropteroylglutamate (H4PteGlu) as coenzymes and catalyzes the reversible interconversion of serine and glycine. In addition to these physiological reactions, SHMT also catalyzes, in the absence of H4PteGlu, the retroaldol cleavage of several 3-hydroxyamino acids, such as allothreonine. Allothreonine is a plant metabolite that appears in the human diet in variable concentrations depending on: plant species, physiological changes during plant growth, senescence, and reactions to environmental stress or to changes due to plant transformation (PMID:10858298, 10952545). Allothreonine is the substrate of the enzyme Serine hydroxymethyltransferase1 (SHMT, EC 2.1.2.1), a human cytoplasmic mRNA binding protein. SHMT uses pyridoxal 5-phosphate (PLP) and tetrahydropteroylglutamate (H4PteGlu) as coenzymes and catalyzes the reversible interconversion of serine and glycine. In addition to these physiological reactions, SHMT also catalyzes, in the absence of H4PteGlu, the retroaldol cleavage of several 3-hydroxyamino acids, such as allothreonine. Allothreonine. CAS Common Chemistry. CAS, a division of the American Chemical Society, n.d. https://commonchemistry.cas.org/detail?cas_rn=144-98-9 (retrieved 2024-07-15) (CAS RN: 144-98-9). Licensed under the Attribution-Noncommercial 4.0 International License (CC BY-NC 4.0). D-Allothreonine is the D type stereoisomer of Allothreonine. D-Allothreonine is a peptido-lipid derived from bacteria. D-Allothreonine, amide-linked to the D-galacturonic acid, is also a constituent in the polysaccharide[1][2]. L-Allothreonine (H-allo-Thr-OH) is an endogenous metabolite.

(±)-erythro-Isoleucine

C6H13NO2 (131.0946238)

(±)-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).

D-Tyrosine

C9H11NO3 (181.0738896)

D-Histidine

C6H9N3O2 (155.06947340000002)

Leucine

C6H13NO2 (131.0946238)

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].

Lysine

C6H14N2O2 (146.1055224)

A diamino acid that is caproic (hexanoic) acid bearing two amino substituents at positions 2 and 6. B - Blood and blood forming organs > B05 - Blood substitutes and perfusion solutions > B05X - I.v. solution additives > B05XB - Amino acids L-lysine is an essential amino acid[1][2] with important roles in connective tissues and carnitine synthesis, energy production, growth in children, and maintenance of immune functions[2]. L-lysine is an essential amino acid[1][2] with important roles in connective tissues and carnitine synthesis, energy production, growth in children, and maintenance of immune functions[2].

L-Cysteic acid

C3H7NO5S (169.0044932)

Cysteinesulfonic acid, also known as (2r)-2-amino-3-sulfopropanoic acid or 3-sulfoalanine, is a member of the class of compounds known as L-alpha-amino acids. L-alpha-amino acids are alpha amino acids which have the L-configuration of the alpha-carbon atom. Cysteinesulfonic acid is soluble (in water) and an extremely strong acidic compound (based on its pKa). Cysteinesulfonic acid can be found in a number of food items such as roman camomile, pili nut, chicory, and garden tomato, which makes cysteinesulfonic acid a potential biomarker for the consumption of these food products.

Lysine

C6H14N2O2 (146.1055224)

B - Blood and blood forming organs > B05 - Blood substitutes and perfusion solutions > B05X - I.v. solution additives > B05XB - Amino acids L-lysine is an essential amino acid[1][2] with important roles in connective tissues and carnitine synthesis, energy production, growth in children, and maintenance of immune functions[2]. L-lysine is an essential amino acid[1][2] with important roles in connective tissues and carnitine synthesis, energy production, growth in children, and maintenance of immune functions[2].

Leucine

C6H13NO2 (131.0946238)

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].

Arginine

C6H14N4O2 (174.1116704)

COVID info from clinicaltrial, clinicaltrials, clinical trial, clinical trials Corona-virus Coronavirus SARS-CoV-2 COVID-19 SARS-CoV COVID19 SARS2 SARS L-Arginine ((S)-(+)-Arginine) is the substrate for the endothelial nitric oxide synthase (eNOS) to generate NO. L-Arginine is transported into vascular smooth muscle cells by the cationic amino acid transporter family of proteins where it is metabolized to nitric oxide (NO), polyamines, or L-proline[1][2]. L-Arginine ((S)-(+)-Arginine) is the substrate for the endothelial nitric oxide synthase (eNOS) to generate NO. L-Arginine is transported into vascular smooth muscle cells by the cationic amino acid transporter family of proteins where it is metabolized to nitric oxide (NO), polyamines, or L-proline[1][2].

HISTIDINE

C6H9N3O2 (155.06947340000002)

L-Histidine is an essential amino acid for infants. L-Histidine is an inhibitor of mitochondrial glutamine transport. L-Histidine is an essential amino acid for infants. L-Histidine is an inhibitor of mitochondrial glutamine transport. L-Histidine is an essential amino acid for infants. L-Histidine is an inhibitor of mitochondrial glutamine transport.

Arginine

C6H14N4O2 (174.1116704)

An alpha-amino acid that is glycine in which the alpha-is substituted by a 3-guanidinopropyl group. COVID info from clinicaltrial, clinicaltrials, clinical trial, clinical trials Corona-virus Coronavirus SARS-CoV-2 COVID-19 SARS-CoV COVID19 SARS2 SARS relative retention time with respect to 9-anthracene Carboxylic Acid is 0.047 relative retention time with respect to 9-anthracene Carboxylic Acid is 0.045 Acquisition and generation of the data is financially supported by the Max-Planck-Society L-Arginine ((S)-(+)-Arginine) is the substrate for the endothelial nitric oxide synthase (eNOS) to generate NO. L-Arginine is transported into vascular smooth muscle cells by the cationic amino acid transporter family of proteins where it is metabolized to nitric oxide (NO), polyamines, or L-proline[1][2]. L-Arginine ((S)-(+)-Arginine) is the substrate for the endothelial nitric oxide synthase (eNOS) to generate NO. L-Arginine is transported into vascular smooth muscle cells by the cationic amino acid transporter family of proteins where it is metabolized to nitric oxide (NO), polyamines, or L-proline[1][2].

Isoleucine

C6H13NO2 (131.0946238)

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.

Histidine

C6H9N3O2 (155.06947340000002)

An alpha-amino acid that is propanoic acid bearing an amino substituent at position 2 and a 1H-imidazol-4-yl group at position 3. The L-enantiomer of the amino acid histidine. Histidine (symbol His or H)[2] is an essential amino acid that is used in the biosynthesis of proteins. It contains an α-amino group (which is in the protonated –NH3+ form under biological conditions), a carboxylic acid group (which is in the deprotonated –COO− form under biological conditions), and an imidazole side chain (which is partially protonated), classifying it as a positively charged amino acid at physiological pH. Initially thought essential only for infants, it has now been shown in longer-term studies to be essential for adults also.[3] It is encoded by the codons CAU and CAC. Histidine was first isolated by Albrecht Kossel and Sven Gustaf Hedin in 1896.[4] The name stems from its discovery in tissue, from ἱστός histós "tissue".[2] It is also a precursor to histamine, a vital inflammatory agent in immune responses. The acyl radical is histidyl. relative retention time with respect to 9-anthracene Carboxylic Acid is 0.046 relative retention time with respect to 9-anthracene Carboxylic Acid is 0.045 relative retention time with respect to 9-anthracene Carboxylic Acid is 0.043 L-Histidine is an essential amino acid for infants. L-Histidine is an inhibitor of mitochondrial glutamine transport. L-Histidine is an essential amino acid for infants. L-Histidine is an inhibitor of mitochondrial glutamine transport. L-Histidine is an essential amino acid for infants. L-Histidine is an inhibitor of mitochondrial glutamine transport.

Aspartic Acid

C4H7NO4 (133.0375062)

An alpha-amino acid that consists of succinic acid bearing a single alpha-amino substituent COVID info from COVID-19 Disease Map, PDB, Protein Data Bank, clinicaltrial, clinicaltrials, clinical trial, clinical trials D018377 - Neurotransmitter Agents > D018846 - Excitatory Amino Acids Corona-virus Coronavirus SARS-CoV-2 COVID-19 SARS-CoV COVID19 SARS2 SARS relative retention time with respect to 9-anthracene Carboxylic Acid is 0.051 relative retention time with respect to 9-anthracene Carboxylic Acid is 0.050 relative retention time with respect to 9-anthracene Carboxylic Acid is 0.054 L-Aspartic acid is is an amino acid, shown to be a suitable proagent for colon-specific agent deliverly. L-Aspartic acid is is an amino acid, shown to be a suitable proagent for colon-specific agent deliverly.

DL-Leucine

C6H13NO2 (131.0946238)

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

C6H13NO2 (131.0946238)

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.

L-Methionine

C5H11NO2S (149.0510466)

The L-enantiomer of methionine. MS2 deconvoluted using MS2Dec from all ion fragmentation data, MetaboLights identifier MTBLS1040; FFEARJCKVFRZRR-BYPYZUCNSA-N_STSL_0047_Methionine_8000fmol_180416_S2_LC02_MS02_69; 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-Methionine is the L-isomer of Methionine, an essential amino acid for human development. Methionine acts as a hepatoprotectant. L-Methionine is the L-isomer of Methionine, an essential amino acid for human development. Methionine acts as a hepatoprotectant.

L-Lysine

C6H14N2O2 (146.1055224)

An L-alpha-amino acid; the L-isomer of lysine. L-lysine is an essential amino acid[1][2] with important roles in connective tissues and carnitine synthesis, energy production, growth in children, and maintenance of immune functions[2]. L-lysine is an essential amino acid[1][2] with important roles in connective tissues and carnitine synthesis, energy production, growth in children, and maintenance of immune functions[2].

L-Arginine

C6H14N4O2 (174.1116704)

An L-alpha-amino acid that is the L-isomer of arginine. MS2 deconvoluted using MS2Dec from all ion fragmentation data, MetaboLights identifier MTBLS1040; ODKSFYDXXFIFQN-BYPYZUCNSA-N_STSL_0099_L-Arginine_8000fmol_180506_S2_LC02_MS02_67; 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-Arginine ((S)-(+)-Arginine) is the substrate for the endothelial nitric oxide synthase (eNOS) to generate NO. L-Arginine is transported into vascular smooth muscle cells by the cationic amino acid transporter family of proteins where it is metabolized to nitric oxide (NO), polyamines, or L-proline[1][2]. L-Arginine ((S)-(+)-Arginine) is the substrate for the endothelial nitric oxide synthase (eNOS) to generate NO. L-Arginine is transported into vascular smooth muscle cells by the cationic amino acid transporter family of proteins where it is metabolized to nitric oxide (NO), polyamines, or L-proline[1][2].

L-Histidine

C6H9N3O2 (155.06947340000002)

MS2 deconvoluted using MS2Dec from all ion fragmentation data, MetaboLights identifier MTBLS1040; HNDVDQJCIGZPNO_STSL_0107_Histidine_8000fmol_180430_S2_LC02_MS02_142; 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-Histidine is an essential amino acid for infants. L-Histidine is an inhibitor of mitochondrial glutamine transport. L-Histidine is an essential amino acid for infants. L-Histidine is an inhibitor of mitochondrial glutamine transport. L-Histidine is an essential amino acid for infants. L-Histidine is an inhibitor of mitochondrial glutamine transport.

L-Allothreonine

C4H9NO3 (119.0582404)

The L-enantiomer of allothreonine. L-Allothreonine (H-allo-Thr-OH) is an endogenous metabolite.

L-Serine

C3H7NO3 (105.0425912)

The L-enantiomer of serine. MS2 deconvoluted using MS2Dec from all ion fragmentation data, MetaboLights identifier MTBLS1040; MTCFGRXMJLQNBG_STSL_0098_Serine_8000fmol_180430_S2_LC02_MS02_174; 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-Serine ((-)-Serine; (S)-Serine), one of the so-called non-essential amino acids, plays a central role in cellular proliferation. L-Serine ((-)-Serine; (S)-Serine), one of the so-called non-essential amino acids, plays a central role in cellular proliferation.

L-Leucine

C6H13NO2 (131.0946238)

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-Tyrosine

C9H11NO3 (181.0738896)

MS2 deconvoluted using MS2Dec from all ion fragmentation data, MetaboLights identifier MTBLS1040; OUYCCCASQSFEME-QMMMGPOBSA-N_STSL_0110_L-Tyrosine_0500fmol_180506_S2_LC02_MS02_57; 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-Tyrosine is a non-essential amino acid which can inhibit citrate synthase activity in the posterior cortex. L-Tyrosine is a non-essential amino acid which can inhibit citrate synthase activity in the posterior cortex.

Cysteic Acid

C3H7NO5S (169.00449319999998)

An amino sulfonic acid that is the sulfonic acid analogue of cysteine.

L-Aspartic Acid

C4H7NO4 (133.0375062)

The L-enantiomer of aspartic acid. MS2 deconvoluted using MS2Dec from all ion fragmentation data, MetaboLights identifier MTBLS1040; CKLJMWTZIZZHCS_STSL_0112_Aspartic acid_2000fmol_180430_S2_LC02_MS02_26; 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-Aspartic acid is is an amino acid, shown to be a suitable proagent for colon-specific agent deliverly. L-Aspartic acid is is an amino acid, shown to be a suitable proagent for colon-specific agent deliverly.

4-Aminobutanoic acid

C4H9NO2 (103.0633254)

2-amino-3-(4-hydroxyphenyl)propanoic acid

C9H11NO3 (181.0738896)

(2S)-6-amino-2-azaniumylhexanoate

C6H14N2O2 (146.1055224)

furoic acid

C3H7NO5S (169.00449319999998)

The L-enantiomer of cysteic acid.

(3r,7e,9s,12e,14s)-14-ethyl-5-hydroxy-5-(hydroxymethyl)-3,7,9,13-tetramethyl-11-methylidene-1-oxacyclotetradeca-7,12-diene-2,4-dione

C21H32O5 (364.2249622)

(3r,5s,7e,9s,12e,14s)-14-ethyl-5-hydroxy-5-(hydroxymethyl)-3,7,9,13-tetramethyl-11-methylidene-1-oxacyclotetradeca-7,12-diene-2,4-dione

C21H32O5 (364.2249622)