NCBI Taxonomy: 5296
Puccinia (ncbi_taxid: 5296)
found 11 associated metabolites at genus taxonomy rank level.
Ancestor: Pucciniaceae
Child Taxonomies: Puccinia codyi, Puccinia drabae, Puccinia poarum, Puccinia hordei, Puccinia sorghi, Puccinia monoica, Puccinia aberrans, Puccinia caricina, Puccinia graminis, Puccinia coronata, Puccinia buxi, Puccinia atra, Puccinia afra, Puccinia vaga, Puccinia carduorum, Puccinia thlaspeos, Puccinia recondita, Puccinia aucta, Puccinia elymi, Puccinia amari, Puccinia porri, Puccinia levis, Puccinia cyani, Puccinia unica, Puccinia mixta, Puccinia macra, Puccinia junci, Puccinia cnici, Puccinia firma, Puccinia ribis, Puccinia lycii, Puccinia ocimi, Puccinia allii, Puccinia consimilis, Puccinia violae, Puccinia jaceae, Puccinia vexans, Puccinia scirpi, Puccinia pascua, Puccinia wiehei, Puccinia iridis, Puccinia cyperi, Puccinia cladii, Puccinia maurea, Puccinia dolosa, Puccinia operta, Puccinia alpina, Puccinia tenuis, Puccinia linkii, Puccinia fumosa, Puccinia vincae, Puccinia morata, Puccinia nitida, Puccinia lobata, Puccinia brachypodii, Puccinia mesnieriana, Puccinia montanensis, Puccinia striiformis, Puccinia xanthii, Puccinia thaliae, Puccinia zoysiae, Puccinia aizazii, Puccinia caricis, Puccinia litseae, Puccinia isiacae, Puccinia menthae, Puccinia dioicae, Puccinia abrupta, Puccinia bassiae, Puccinia duthiae, Puccinia liberta, Puccinia virgata, Puccinia silphii, Puccinia pygmaea, Puccinia similis, Puccinia kuehnii, Puccinia horiana, Puccinia rufipes, Puccinia cenchri, Puccinia bromina, Puccinia holcina, Puccinia tulipae, Puccinia cesatii, Puccinia stipina, Puccinia paspali, Puccinia rapipes, Puccinia clavata, Puccinia tiritea, Puccinia calthae, Puccinia jasmini, Puccinia salviae, Puccinia luzulae, Puccinia asteris, Puccinia limosae, Puccinia obtecta, Puccinia turgida, Puccinia emiliae, Puccinia kusanoi, Puccinia funkiae, Puccinia asarina, Puccinia akiraho, Puccinia obscura, Puccinia oxyriae, Puccinia salihae, Puccinia smilacis, Puccinia cygnorum, Puccinia cribrata, Puccinia carissae, Puccinia polysora, Puccinia purpurea, Puccinia pammelii, Puccinia boroniae, Puccinia scleriae, Puccinia setariae, Puccinia digitata, Puccinia doidgeae, Puccinia stobaeae, Puccinia modiolae, Puccinia abrotani, Puccinia tuberosa, Puccinia epigejos, Puccinia festucae, Puccinia dispersa, Puccinia dietelii, Puccinia abnormis, Puccinia imposita, Puccinia insolita, Puccinia tubulosa, Puccinia crupinae, Puccinia antenori, Puccinia vivipari, Puccinia gigantea, Puccinia acetosae, Puccinia recedens, Puccinia paludosa, Puccinia lapsanae, Puccinia hieracii, Puccinia serpylli, Puccinia parkerae, Puccinia marrubii, Puccinia ludwigii, Puccinia velutina, Puccinia maculosa, Puccinia conclusa, Puccinia oxalidis, Puccinia bupleuri, Puccinia galiorum, Puccinia enceliae, Puccinia cacabata, Puccinia colossea, Puccinia stylidii, Puccinia bardanae, Puccinia mikaniae, Puccinia pampeana, Puccinia gilgiana, Puccinia ursiniae, Puccinia circaeae, Puccinia urticata, Puccinia dulichii, Puccinia karelica, Puccinia suzutake, Puccinia galeniae, Puccinia sessilis, Puccinia asparagi, Puccinia chunjiei, Puccinia tanaceti, Puccinia carthami, Puccinia elaeagni, Puccinia erianthi, Puccinia impedita, Puccinia lantanae, Puccinia ellisiana, Puccinia comandrae, Puccinia nishidana, Puccinia agrophila, Puccinia cumminsii, Puccinia sporoboli, Puccinia rhagodiae, Puccinia moiwensis, Puccinia cf. allii, Puccinia emaculata, Puccinia caulicola, Puccinia gibberosa, Puccinia heucherae, Puccinia subalpina, Puccinia wyomensis, Puccinia oncospora, Puccinia maureanui, Puccinia miscanthi, Puccinia oahuensis, Puccinia trebouxii, Puccinia albescens, Puccinia wolgensis, Puccinia paspalina, Puccinia acroptili, Puccinia argentata, Puccinia komarovii, Puccinia rupestris, Puccinia uliginosa, Puccinia uniporula, Puccinia eriophori, Puccinia phlomidis, Puccinia angustata, Puccinia hysterium, Puccinia gansensis, Puccinia morrisoni, Puccinia atrofusca, Puccinia morthieri, Puccinia albispora, Puccinia bistortae, Puccinia pazschkei, Puccinia aegopodii, Puccinia vaginatae, Puccinia dianellae, Puccinia saccardoi, Puccinia microsora, Puccinia justiciae, Puccinia dimidipes, Puccinia silvatica, Puccinia lateritia, Puccinia dampierae, Puccinia bolleyana, Puccinia haemodori, Puccinia tumidipes, Puccinia mellifera, Puccinia urbaniana, Puccinia aridariae, Puccinia arachidis, Puccinia patriniae, Puccinia arenariae, Puccinia distincta, Puccinia paederiae, Puccinia triticina, Puccinia otzeniani, Puccinia chloridis, Puccinia latimamma, Puccinia tokyensis, Puccinia helianthi, Puccinia peperomiae, Puccinia adenocauli, Puccinia phaeospora, Puccinia physalidis, Puccinia phragmitis, Puccinia dichondrae, Puccinia cynodontis, Puccinia magnusiana, Puccinia grevilleae, Puccinia lasiacidis, Puccinia novopanici, Puccinia windsoriae, Puccinia pappophori, Puccinia tirolensis, Puccinia lippiivora, Puccinia versicolor, Puccinia saxifragae, Puccinia engleriana, Puccinia crandallii, Puccinia cancellata, Puccinia plagianthi, Puccinia circumdata, Puccinia persistens, Puccinia balsamitae, Puccinia agropyrina, Puccinia perplexans, Puccinia juncophila, Puccinia unciniarum, Puccinia albulensis, Puccinia verbesinae, Puccinia nigrescens, Puccinia melampodii, Puccinia seijoensis, Puccinia littoralis, Puccinia antirrhini, Puccinia suaveolens, Puccinia senecionis, Puccinia commelinae, Puccinia calthicola, Puccinia parnassiae, Puccinia virgaureae, Puccinia globosipes, Puccinia lophatheri, Puccinia millefolii, Puccinia conoclinii, Puccinia xanthosiae, Puccinia convolvuli, Puccinia tageticola, Puccinia substriata, Puccinia platyspora, Puccinia nepalensis, Puccinia pittieriana, Puccinia spegazzinii, Puccinia longicornis, Puccinia psychotriae, Puccinia ferruginosa, Puccinia arthrocnemi, Puccinia liliacearum, Puccinia gastrolobii, Puccinia caulophylli, Puccinia pimpinellae, Puccinia esclavensis, Puccinia graminicola, Puccinia merrilliana, Puccinia tatarinovii, Puccinia millegranae, Puccinia pritzeliana, Puccinia peradeniyae, Puccinia myrsiphylli, Puccinia thunbergiae, Puccinia aff. scirpi, Puccinia rangiferina, Puccinia dactylidina, Puccinia pileiformis, Puccinia cannacearum, Puccinia durangensis, Puccinia malvacearum, Puccinia heeringiana, Puccinia digraphidis, Puccinia calcitrapae, Puccinia scorodoniae, Puccinia glechomatis, Puccinia fergussonii, Puccinia baccharidis, Puccinia impatientis, Puccinia minutissima, Puccinia irrequisita, Puccinia scorzonerae, Puccinia mysuruensis, Puccinia tillandsiae, Puccinia tetragoniae, Puccinia euphrasiana, Puccinia hectorensis, Puccinia heterogenea, Puccinia heterospora, Puccinia sherardiana, Puccinia cf. limosae, Puccinia klugkistiana, Puccinia nakanishikii, Puccinia coleataeniae, Puccinia loranthicola, Puccinia chondrillina, Puccinia bartholomaei, Puccinia xinyuanensis, Puccinia arrhenatheri, Puccinia arundinariae, Puccinia berkheyicola, Puccinia chaetochloae, Puccinia punctiformis, Puccinia artemisiella, Puccinia miscanthidii, Puccinia ballotiflora, Puccinia hibayamensis, Puccinia hydrocotyles, Puccinia eleocharidis, unclassified Puccinia, Puccinia cymbopogonis, Puccinia chrysanthemi, Puccinia paradoxapoda, Puccinia dracunculina, Puccinia pentstemonis, Puccinia lagenophorae, Puccinia andropogonis, Puccinia osoyoosensis, Puccinia canaliculata, Puccinia aff. obscura, Puccinia galiiuniversa, Puccinia flavenscentis, Puccinia geitonoplesii, Puccinia gnaphaliicola, Puccinia hypochoeridis, Puccinia crotonopsidis, Puccinia sparganioidis, Puccinia symphoricarpi, Puccinia actaeae-elymi, Puccinia melanocephala, Puccinia penicillariae, Puccinia nigrolinearis, Puccinia rhei-undulati, Puccinia wahlenbergiae, Puccinia chrysosplenii, Puccinia angustatoides, Puccinia leonotidicola, Puccinia jogashimensis, Puccinia windhoekensis, Puccinia mcclatchieana, Puccinia chardoniensis, Puccinia muehlenbeckiae, Puccinia rhaphidophorae, Puccinia caricis-violae, Puccinia striiformoides, Puccinia pringsheimiana, Puccinia balsamorrhizae, Puccinia pseudodigitata, Puccinia caricis-fediae, Puccinia caricis-gibbae, Puccinia cnici-oleracei, Puccinia geranii-pilosi, Puccinia ribis-pendulae, Puccinia poae-nemoralis, Puccinia fimbristylidis, Puccinia urticae-hirtae, Puccinia urticae-acutae, Puccinia ribis-japonici, Puccinia hemerocallidis, Puccinia elymi-albispora, Puccinia luzulae-maximae, Puccinia septentrionalis, Puccinia meyeri-albertii, Puccinia ribesii-caricis, Puccinia urticae-caricis, Puccinia hordei-secalini, Puccinia knersvlaktensis, Puccinia mesembryanthemi, Puccinia phyllostachydis, Puccinia coronati-hordei, Puccinia aff. verbesinae, Puccinia vernoniae-mollis, Puccinia caricis-stipatae, Puccinia mariae-wilsoniae, Puccinia circaeae-caricis, Puccinia caricis-lactucae, Puccinia caricis-ribicola, Puccinia arrhenathericola, Puccinia ampliaticoronata, Puccinia digitaticoronata, Puccinia eleganticoronata, Puccinia caricis-smilacis, Puccinia caricis-montanae, Puccinia urticae-inflatae, Puccinia eriophori-alpini, Puccinia actaeae-agropyri, Puccinia cf. osoyoosensis, Puccinia aff. calcitrapae, Puccinia caricis-rafaensis, Puccinia pseudostriiformis, Puccinia crepidis-montanae, Puccinia agropyri-ciliaris, Puccinia pseudomesnieriana, Puccinia polygoni-amphibii, Puccinia coronati-japonica, Puccinia caricis-artemisiae, Puccinia caricis-pediformis, Puccinia pelargonii-zonalis, Puccinia caricis-hebeiensis, Puccinia caricis-jilinensis, Puccinia ramificatacoronata, Puccinia cf. psidii AE-2014, Puccinia crepidis-japonicae, Puccinia caricis-tenuiformis, Puccinia cardui-pycnocephali, Puccinia urticae-acutiformis, Puccinia linosyridis-caricis, Puccinia caricis-petasitidis, Puccinia caricis-shepherdiae, Puccinia achnatheri-sibirici, Puccinia infra-aequatorialis, Puccinia coronati-brevispora, Puccinia coronati-longispora, Puccinia coronati-agrostidis, Puccinia aff. cnici-oleracei, Puccinia caricis-atractylodes, Puccinia protuberanticoronata, Puccinia artemisiae-maritimae, Puccinia cerinthes-agropyrina, Puccinia eupatorii-columbiani, Puccinia artemisiae-keiskeanae, Puccinia veronicae-longifoliae, Puccinia aff. coronata ML-2011, Puccinia aff. geranii DAR75671, Puccinia caricis-macrocephalae, Puccinia caricis-siderostictae, Puccinia cf. helianthi WM 3524, Puccinia senecionis-acutiformis, Puccinia ribesii-diversicoloris, Puccinia oenanthes-stoloniferae, Puccinia ribis-nigri-paniculatae, Puccinia calystegiae-soldanellae, Puccinia cf. scirpi OTU 2 SH-2021, Puccinia coronati-calamagrostidis, Puccinia aff. cyperi OTU 1 SH-2021, Puccinia aff. dioicae OTU 2 SH-2021, Puccinia aff. dioicae OTU 3 SH-2021, Puccinia aff. dioicae OTU 4 SH-2021, Puccinia aff. dioicae OTU 5 SH-2021, Puccinia aff. dioicae OTU 6 SH-2021, Puccinia aff. dioicae OTU 8 SH-2021, Puccinia aff. dioicae OTU 9 SH-2021, Puccinia aff. asteris OTU 1 SH-2021, Puccinia aff. asteris OTU 2 SH-2021, Puccinia aff. asteris OTU 3 SH-2021, Puccinia cf. caricina OTU 1 SH-2021, Puccinia cf. caricina OTU 2 SH-2021, Puccinia cf. caricina OTU 3 SH-2021, Puccinia cf. caricina OTU 4 SH-2021, Puccinia cf. caricina OTU 5 SH-2021, Puccinia cf. caricina OTU 6 SH-2021, Puccinia cf. caricina OTU 7 SH-2021, Puccinia cf. caricina OTU 8 SH-2021, Puccinia cf. caricina OTU 9 SH-2021, Puccinia cf. urticata OTU 1 SH-2021, Puccinia cf. urticata OTU 2 SH-2021, Puccinia cf. urticata OTU 3 SH-2021, Puccinia cf. urticata OTU 4 SH-2021, Puccinia aff. dioicae OTU 10 SH-2021, Puccinia cf. caricina OTU 10 SH-2021, Puccinia cf. angustata OTU 3 SH-2021, Puccinia aff. hieracii OTU 1 SH-2021, Puccinia aff. hieracii OTU 2 SH-2021, Puccinia aff. maculosa OTU 1 SH-2021, Puccinia aff. maculosa OTU 2 SH-2021, Puccinia aff. angustata OTU 1 SH-2021, Puccinia aff. angustata OTU 2 SH-2021, Puccinia aff. angustata OTU 3 SH-2021, Puccinia aff. angustata OTU 4 SH-2021, Puccinia aff. bolleyana OTU 1 SH-2021, Puccinia aff. bolleyana OTU 2 SH-2021, Puccinia aff. eriophori OTU 1 SH-2021, Puccinia aff. eriophori OTU 2 SH-2021, Puccinia aff. juncophila OTU 1 SH-2021, Puccinia cf. karelica subsp. laurentina, Puccinia aff. canaliculata OTU 2 SH-2021, Puccinia aff. eleocharidis OTU 1 SH-2021, Puccinia aff. eleocharidis OTU 2 SH-2021
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-Histidine
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-Allothreonine
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.
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].
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].
Arginine
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].
Arginine
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].
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-Histidine
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
The L-enantiomer of allothreonine. L-Allothreonine (H-allo-Thr-OH) is an endogenous metabolite.
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].