Names | |||
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Preferred IUPAC name (2S)-3-(2-Sulfanylidene-2,3-dihydro-1H-imidazol-4-yl)-2-(trimethylazaniumyl)propanoate | |||
Other names L-Ergothioneine; (+)-Ergothioneine; Thiasine; Sympectothion; Ergothionine; Erythrothioneine; Thiolhistidinebetaine | |||
Identifiers | |||
3D model (JSmol) | |||
ChEBI | |||
ChemSpider | |||
ECHA InfoCard | 100.007.131 | ||
KEGG | |||
PubChem CID | |||
UNII | |||
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Properties | |||
C9H15N3O2S | |||
Molar mass | 229.30 g/mol | ||
Appearance | white solid | ||
Melting point | 275 to 277 °C (527 to 531 °F; 548 to 550 K) | ||
Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa). |
Ergothioneine is a naturally occurring amino acid and is a thiourea derivative of histidine, containing a sulfur atom on the imidazole ring. [1] This compound occurs in relatively few organisms, notably actinomycetota, cyanobacteria, and certain fungi. [2] [3] Ergothioneine was discovered by Charles Tanret in 1909 and named after the ergot fungus from which it was first purified, [4] with its structure being determined in 1911. [5] [6]
In humans, ergothioneine is acquired exclusively through the diet and accumulates in erythrocytes, bone marrow, liver, kidney, seminal fluid, and eyes. [7] Although the effect of ergothioneine in vivo is under preliminary research, its physiological role in humans is unknown. [7] Ergothioneine is sold as a dietary supplement. [8]
Ergothioneine has been found in bacteria, plants, and animals, sometimes at millimolar levels. [9] Foods found to contain ergothioneine include liver, kidney, black beans, kidney bean, and oat bran, with the highest levels in bolete and oyster mushrooms. [9] [10] Levels can be variable, even within species and some tissues can contain much more than others. In the human body, the largest amounts of ergothioneine are found in erythrocytes, eye lens, semen, [6] and skin. [11]
Although many species contain ergothioneine, only a few make it; the others absorb it from their diet or, in the case of plants, from their environment. [12] Biosynthesis has been detected in Actinomycetota, such as Mycobacterium smegmatis and certain fungi, such as Neurospora crassa . [2]
The metabolic pathway to produce ergothioneine starts with the methylation of histidine to produce histidine betaine (hercynine). The sulfur atom is then incorporated from cysteine. [9] [13] The biosynthetic genes of ergothioneine have been described in Mycobacterium smegmatis , [14] Neurospora crassa , [15] and Schizosaccharomyces pombe . [16]
Other species of bacteria, such as Bacillus subtilis , Escherichia coli , Proteus vulgaris , and Streptococcus , as well as fungi in the Saccharomycotina cannot make ergothioneine. [17] [18]
Ergothioneine is a thiourea derivative of the betaine of histidine and contains a sulfur atom bonded to the 2-position of the imidazole ring. [19] Typical of thioureas, ergothioneine is less reactive than typical thiols such as glutathione towards alkylating agents like maleimides. It also resists oxidation by air. [9] However, ergothioneine can be slowly oxidized over several days to the disulfide form in acidic solutions. [20]
Various derivatives of ergothioneine have been reported in the literature, such as S-methyl-ergothioneine [21] or selenium-containing selenoneine. [22]
Although potential effects of ergothioneine are under preliminary research, its physiological role in vivo has not been determined. [1] [7]
The Panel on Dietetic Products for the European Food Safety Authority reported safe daily limits of 2.82 mg/kg of body weight for infants, 3.39 mg/kg for small children, and 1.31 mg/kg for adults, including pregnant and breastfeeding women. [8]
Antioxidants are compounds that inhibit oxidation, a chemical reaction that can produce free radicals. Autoxidation leads to degradation of organic compounds, including living matter. Antioxidants are frequently added to industrial products, such as polymers, fuels, and lubricants, to extend their usable lifetimes. Foods are also treated with antioxidants to forestall spoilage, in particular the rancidification of oils and fats. In cells, antioxidants such as glutathione, mycothiol or bacillithiol, and enzyme systems like superoxide dismutase, can prevent damage from oxidative stress.
Methionine is an essential amino acid in humans.
Histidine (symbol His or H) 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. It is encoded by the codons CAU and CAC.
Coenzyme A (CoA, SHCoA, CoASH) is a coenzyme, notable for its role in the synthesis and oxidation of fatty acids, and the oxidation of pyruvate in the citric acid cycle. All genomes sequenced to date encode enzymes that use coenzyme A as a substrate, and around 4% of cellular enzymes use it (or a thioester) as a substrate. In humans, CoA biosynthesis requires cysteine, pantothenate (vitamin B5), and adenosine triphosphate (ATP).
Lipoic acid (LA), also known as α-lipoic acid, alpha-lipoic acid (ALA) and thioctic acid, is an organosulfur compound derived from caprylic acid (octanoic acid). ALA is made in animals normally, and is essential for aerobic metabolism. It is also manufactured and is available as a dietary supplement in some countries where it is marketed as an antioxidant, and is available as a pharmaceutical drug in other countries. Lipoate is the conjugate base of lipoic acid, and the most prevalent form of LA under physiological conditions. Only the (R)-(+)-enantiomer (RLA) exists in nature and is essential for aerobic metabolism because RLA is an essential cofactor of many enzyme complexes.
Metallothionein (MT) is a family of cysteine-rich, low molecular weight proteins. They are localized to the membrane of the Golgi apparatus. MTs have the capacity to bind both physiological and xenobiotic heavy metals through the thiol group of its cysteine residues, which represent nearly 30% of its constituent amino acid residues.
N-Acetylglutamate synthase (NAGS) is an enzyme that catalyses the production of N-acetylglutamate (NAG) from glutamate and acetyl-CoA.
Phosphoribosyl pyrophosphate (PRPP) is a pentose phosphate. It is a biochemical intermediate in the formation of purine nucleotides via inosine-5-monophosphate, as well as in pyrimidine nucleotide formation. Hence it is a building block for DNA and RNA. The vitamins thiamine and cobalamin, and the amino acid tryptophan also contain fragments derived from PRPP. It is formed from ribose 5-phosphate (R5P) by the enzyme ribose-phosphate diphosphokinase:
Gliotoxin is a sulfur-containing mycotoxin that belongs to a class of naturally occurring 2,5-diketopiperazines produced by several species of fungi, especially those of marine origin. It is the most prominent member of the epipolythiopiperazines, a large class of natural products featuring a diketopiperazine with di- or polysulfide linkage. These highly bioactive compounds have been the subject of numerous studies aimed at new therapeutics. Gliotoxin was originally isolated from Gliocladium fimbriatum, and was named accordingly. It is an epipolythiodioxopiperazine metabolite that is one of the most abundantly produced metabolites in human invasive Aspergillosis (IA).
The enzyme 3-dehydroquinate dehydratase (EC 4.2.1.10) catalyzes the chemical reaction
The enzyme chorismate synthase catalyzes the chemical reaction
In enzymology, a cystathionine gamma-synthase is an enzyme that catalyzes the formation of cystathionine from cysteine and an activated derivative of homoserine, e.g.:
Peroxiredoxin-6 is a protein that in humans is encoded by the PRDX6 gene. It is a member of the peroxiredoxin family of antioxidant enzymes.
Multienzyme complex contains several copies of one or several enzymes packed into one assembly. Multienzyme complex carries out a single or a series of biochemical reactions taking place in the cells. It allows to segregate certain biochemical pathways into one place in the cell.
The α-aminoadipate pathway is a biochemical pathway for the synthesis of the amino acid L-lysine. In the eukaryotes, this pathway is unique to several species of yeast, higher fungi, and the euglenids. It has also been reported from bacteria of the genus Thermus and also in Pyrococcus horikoshii, potentially suggesting a wider distribution than previously thought. This uniqueness of the pathway makes it a potentially interesting target for antimycotics.
Selenium yeast is a feed additive for livestock, used to increase the selenium content in their fodder. It is a form of selenium currently approved for human consumption in the EU and Britain. Inorganic forms of selenium are used in feeds. Since these products can be patented, producers can demand premium prices. It is produced by fermenting Saccharomyces cerevisiae in a selenium-rich media.
Dr. Claus Jacob B.Sc. M.A. D.Phil. (Oxon) FRSC CChem is a German scientist and politician functioning as the Head of Bioorganic Chemistry, School of Pharmacy, Saarland University and a member of the Ecological Democratic Party (ÖDP) and represents the Family Party of Germany in the Orstrat Hassel / Saar. He is currently a candidate to the Bundestag on behalf of ÖDP, Homburg constituency. Jacob is known to many of his students as Professor Claus rather than Professor Jacob. This is due to cultural reasons stemming from the rich international environment of his research team and Global collaborations. He received his B.Sc.(Hons) 1st class in Chemistry in 1993 from the University of Leicester, England and his D.Phil. (Oxon) from the University of Oxford in 1997. Jacob had interests in education, psychology, history and philosophy and was awarded a Magister Artium from the University of Hagen in 1998. He is an expert in a variety of topics ranging from organic synthesis, bioorganic chemistry, catalytic sensor/effector agents, intracellular diagnostics, nanotechnology, natural products, reactive sulfur and selenium species, and redox regulation via the cellular thiolstat. He has contributed more than 200 publications to the previously mentioned fields.
Meleagrin and its derivatives such as oxaline are bio-active benzylisoquinoline alkaloids made by various species of Penicillium fungi. It is similar to other fungal alkaloids, such as Roquefortine C, which is made as an intermediate in the same biosynthetic pathway.
White Collar-1 (wc-1) is a gene in Neurospora crassa encoding the protein WC-1. WC-1 has two separate roles in the cell. First, it is the primary photoreceptor for Neurospora and the founding member of the class of principle blue light photoreceptors in all of the fungi. Second, it is necessary for regulating circadian rhythms in FRQ. It is a key component of a circadian molecular pathway that regulates many behavioral activities, including conidiation. WC-1 and WC-2, an interacting partner of WC-1, comprise the White Collar Complex (WCC) that is involved in the Neurospora circadian clock. WCC is a complex of nuclear transcription factor proteins, and contains transcriptional activation domains, PAS domains, and zinc finger DNA-binding domains (GATA). WC-1 and WC-2 heterodimerize through their PAS domains to form the White Collar Complex (WCC).
Selenoneine is a selenium containing ergothioneine derivative where the selenium (Se) atom replaces a sulfur atom. It can be systematically named as.