497-30-3 Usage
Description
L-(+)-Ergothioneine is a naturally-occurring amino acid derived from histidine via hercynine. Ergothioneine is a stable antioxidant that scavenges and detoxifies free radicals and oxidants, increases intracellular thiol levels, controls nuclear factor-κB activation, and inhibits inflammatory gene expression. In addition, it inhibits the peroxynitrite-dependent nitration of nitrotyrosine, blocks oxidative DNA damage and cell death, and prevents the formation of xanthine and hypoxanthine. Ergothioneine is transported by the organic cation/carnitine transporter 1, which has been linked with autoimmune diseases, including rheumatoid arthritis and Crohn’s disease.
Chemical Properties
White Solid
Uses
L-(+)-Ergothioneine is a natural molecule isolated from the rye ergot fungus and later identified in rat erythrocytes and liver and in numerous other animal tissues. Its antioxidizing properties may afford the compound therapeutic potential or it may be used as a food additive or in cosmetics.
benefits
L-(+)-Ergothioneine is a natural antioxidant, which has various physiological functions such as scavenging free radicals, detoxification, maintaining DNA biosynthesis, normal cell growth and cellular immunity.
General Description
L-(+)-Ergothioneine (ET) is a sulfur-containing amino acid, which is only produced by Actinomycetales bacteria and non-yeast like fungi belonging to the division Basidiomycota and Ascomycota. It was originally isolated from Claviceps purpurea or rye ergot. It is obtained from L-histidine, which is converted into betaine form called hercynine. It is found in both animals and plants, and mammals usually obtain it from their diet, e.g. through mushrooms or oats. It is tautomeric in nature, and in neutral aqueous solution exists in thione form.
Biochem/physiol Actions
L-(+)-Ergothioneine (ET) has the maximum concentrations in tissues subjected to oxidative stress, with the highest being in blood, eye lens, bone marrow, semen and liver. It acts as an anti-oxidant and prevents apoptosis, by scavenging reactive oxygen and nitrogen species. The anti-oxidant activity is attributable to sulfhydryl groups. It acts as a substrate for SLC22A4 (solute carrier family 22, member 4) transporter. In alveolar macrophages, it prevents the release of interleukin-8 (IL-8) by tumor necrosis factor (TNF)α. IL-8 is an inflammatory cytokine. It also regulates the oxidative damage in liver and kidneys, and has a protective action against lipid peroxidation. It is also responsible for the conservation of endogenous glutathione and α-tocopherol. ET being an antioxidant, protects against γ and UV radiation. In UV-irradiated human dermal fibroblasts, it scavenges reactive oxygen species (ROS), and suppresses matrix metalloproteinases 1 (MMP1) expression. It might also have anti-ageing effects on skin caused by UV-radiation.
Check Digit Verification of cas no
The CAS Registry Mumber 497-30-3 includes 6 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 3 digits, 4,9 and 7 respectively; the second part has 2 digits, 3 and 0 respectively.
Calculate Digit Verification of CAS Registry Number 497-30:
(5*4)+(4*9)+(3*7)+(2*3)+(1*0)=83
83 % 10 = 3
So 497-30-3 is a valid CAS Registry Number.
InChI:InChI=1/C9H15N3O2S/c1-12(2,3)7(8(13)14)4-6-5-10-9(15)11-6/h5,7H,4H2,1-3H3,(H2-,10,11,13,14,15)/t7-/m0/s1
497-30-3Relevant articles and documents
Synthesis method of ergothioneine
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Paragraph 0007; 0037-0038, (2020/09/09)
The invention provides a synthesis method and an intermediate of ergothioneine. According to the method, chirality is introduced in a chiral catalysis mode, reaction intermediates can be dissolved inan organic solvent, high-purity ergothioneine can be conveniently obtained at a low cost, reaction conditions are mild, control is easy, environmental pollution is small, and the method can better adapt to industrial production.
Snapshots of C-S Cleavage in Egt2 Reveals Substrate Specificity and Reaction Mechanism
Irani, Seema,Naowarojna, Nathchar,Tang, Yang,Kathuria, Karan R.,Wang, Shu,Dhembi, Anxhela,Lee, Norman,Yan, Wupeng,Lyu, Huijue,Costello, Catherine E.,Liu, Pinghua,Zhang, Yan Jessie
, p. 519 - 4,529 (2018/03/06)
Sulfur incorporation in the biosynthesis of ergothioneine, a histidine thiol derivative, differs from other well-characterized transsulfurations. A combination of a mononuclear non-heme iron enzyme-catalyzed oxidative C-S bond formation and a subsequent pyridoxal 5′-phosphate (PLP)-mediated C-S lyase reaction leads to the net transfer of a sulfur atom from a cysteine to a histidine. In this study, we structurally and mechanistically characterized a PLP-dependent C-S lyase Egt2, which mediates the sulfoxide C-S bond cleavage in ergothioneine biosynthesis. A cation-π interaction between substrate and enzyme accounts for Egt2's preference of sulfoxide over thioether as a substrate. Using mutagenesis and structural biology, we captured three distinct states of the Egt2 C-S lyase reaction cycle, including a labile sulfenic intermediate captured in Egt2 crystals. Chemical trapping and high-resolution mass spectrometry were used to confirm the involvement of the sulfenic acid intermediate in Egt2 catalysis. Irani et al. have determined the structure of Egt2, a C-S lyase at the final step in the ergothioneine biosynthesis pathways. Using X-ray crystallography and various biochemical studies, the reaction mechanism was delineated.
Bioinformatic and biochemical characterizations of C-S bond formation and cleavage enzymes in the fungus neurospora crassa ergothioneine biosynthetic pathway
Hu, Wen,Song, Heng,Her, Ampon Sae,Bak, Daniel W.,Naowarojna, Nathchar,Elliott, Sean J.,Qin, Li,Chen, Xiaoping,Liu, Pinghua
supporting information, p. 5382 - 5385 (2015/02/19)
Ergothioneine is a histidine thiol derivative. Its mycobacterial biosynthetic pathway has five steps (EgtA-E catalysis) with two novel reactions: a mononuclear nonheme iron enzyme (EgtB) catalyzed oxidative C-S bond formation and a PLP-mediated C-S lyase (EgtE) reaction. Our bioinformatic and biochemical analyses indicate that the fungus Neurospora crassa has a more concise ergothioneine biosynthetic pathway because its nonheme iron enzyme, Egt1, makes use of cysteine instead of γ-Glu-Cys as the substrate. Such a change of substrate preference eliminates the competition between ergothioneine and glutathione biosyntheses. In addition, we have identi fied the N. crassa C-S lyase (NCU11365) and reconstituted its activity in vitro, which makes the future ergothioneine production through metabolic engineering feasible. (Chemical Equation Presented).
