Biosynthesis of Ergothioneine and Hercynine by Fungi and
            <i>Actinomycetales</i>

Genghof, Dorothy S.

doi:10.1128/jb.103.2.475-478.1970

Cited by 98 publications

(62 citation statements)

References 13 publications

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“…Ergothioneine is synthesized by a wide variety of fungi (Genghof, 1970) and is assimilated by higher plants (Melville, 1958;Audley and Tan, 1968) and many animals, including man (Stowell, 1961). Ergothioneine in mammals is not degraded but stored in near millimolar amounts in the liver, red blood cells, bone marrow, and seminal vesicles, and micromolar levels in the central nervous system (references in Hartman and Hartman, 1987).…”

Section: Discussionmentioning

confidence: 99%

Some Prevalent Biomolecules as Defenses Against Singlet Oxygen Damage

Midden

1988

Photochem & Photobiology

165

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We have compared the relative abilities of some putative biological protectors to block oxidation of 2,5-bis(hydroxymethyl)furan (BHMF)? in illuminated solutions containing the photosensitizer rose bengal and in the separated-surface-sensitizer (S-S-S) system involving pure singlet oxygen ('ASO2). While L-histidine is a well-known quencher of singlet oxygen, free L-histidine is not commonly found in high concentrations in nature. L-Carnosine (P-alanyl-L-histidine), however, is present in the striated muscles of many organisms, most notably mammals, in concentrations up to 40 mM. At neutral pH, carnosine quenched singlet oxygen more effectively than did equimolar histidine. both in solubilized sensitizer studies and in the S-S-S system. In the pure singlet oxygen system. 1 mM carnosine reduced the rate of BHMF oxidation as effectively as 3 mM histidine alone, or a mixture of 3 mM histidine and 3 mM (3-alanine. The fungal product L-ergothioneine (2-thiol-t.-histidine betaine) and its synthetic analogue, 2-thiolhistidine, at 1 mM blocked photosensitized BHMF oxidation using solubilized rose bengal, as did urate at 0.5 mM. All three compounds failed to reduce the rate of BHMF Oxidation by singlet oxygen in the S-S-S system, however. Homocarnosine (y-aminobutyryl-Lhistidine) gave levels of protection against BHMF oxidation identical to histidine, but is present in the central nervous system only at micromolar concentrations. Neither I mM imidazole nor 5 mM urea reduced BHMF oxidation in either system. We conclude that some prevalent biomolecules may afford protection either by preventing singlet oxygen production (urate, L-ergothioneine) or by intercepting singlet oxygen once formed (L-carnosine).

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Section: Discussionmentioning

confidence: 99%

Some Prevalent Biomolecules as Defenses Against Singlet Oxygen Damage

Midden

1988

Photochem & Photobiology

165

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“…Unlike MSH, ESH has been detected in plants, fungi, animals and bacteria. However, only fungi and actinomycetes are able to synthesize this thiol (Genghof, 1970). The amount of ESH present in actinomycetes is ten-fold lower than that of MSH and its exact function in these bacteria is unknown (Fahey, 2001).…”

Section: Introductionmentioning

confidence: 99%

Mycothiol-dependent proteins in actinomycetes

Rawat¹,

Av‐Gay²

2007

FEMS Microbiol Rev

107

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The pseudodisaccharide mycothiol is present in millimolar levels as the dominant thiol in most species of Actinomycetales. The primary role of mycothiol is to maintain the intracellular redox homeostasis. As such, it acts as an electron acceptor/donor and serves as a cofactor in detoxification reactions for alkylating agents, free radicals and xenobiotics. In addition, like glutathione, mycothiol may be involved in catabolic processes with an essential role for growth on recalcitrant chemicals such as aromatic compounds. Following a little over a decade of research since the discovery of mycothiol in 1994, we summarize the current knowledge about the role of mycothiol as an enzyme cofactor and consider possible mycothiol-dependent enzymes.

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“…To this end, we have engineered Saccharomyces cerevisiae for the production of ergothioneine, reaching levels of 0.6 g/L. As there are many different organisms that produce ergothioneine (Genghof, 1970; Genghof et al, 1956; Genghof and Vandamme, 1964; Kalaras et al, 2017; Pfeiffer et al, 2011; Pluskal et al, 2014; Seebeck, 2010; Sheridan et al, 2016; Tanret, 1909) (supplementary table 9 and 10), we have focused on the organisms in which genes for ergothioneine production were identified. Other heterologous or from different organisms could therefore also be tested in S. cerevisiae to potentially find better performing combinations than those described here.…”

Section: Discussionmentioning

confidence: 99%

“…Ergothioneine was discovered in 1909 in the ergot fungus Claviceps purpurea (Tanret, 1909), and its structure was determined two years later (Barger and Ewins, 1911). Subsequently, several other organisms were found to produce ergothioneine, including the filamentous fungus Neurospora crassa (Genghof et al, 1956), the yeast Schizosaccharomyces pombe (Pluskal et al, 2014), various actinobacteria (Genghof, 1970) including Mycobacterum smegmatis (Seebeck, 2010), and in particular various basidiomycetes (mushrooms) (Genghof, 1970).…”

Section: Introductionmentioning

confidence: 99%

Engineering the yeastSaccharomyces cerevisiaefor the production of L-(+)-ergothioneine

Hoek

Darbani

Zugaj

et al. 2019

Preprint

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20 cerevisiae, yeast, nutraceutical 21 22 Abbreviations: ERG L-(+)-ergothioneine, HCO S-(hercyn-2-yl)-L-cysteine S-oxide, PBS 23 phosphate-buffered saline, PI propidium iodide, PLP pyridoxal 5'-phosphate, SAM S-adenosyl-24 L-methionine 25 26Abstract 27 L-(+)-Ergothioneine is an unusual, naturally occurring antioxidant nutraceutical that has been 28 shown to help reduce cellular oxidative damage. Humans do not biosynthesise it, so can acquire 29 it only from their diet; it exploits a specific transporter (SLC22A4) for its uptake. ERG is 30 considered to be a nutraceutical and possible vitamin that is involved in the maintenance of 31 health, and seems to be at too low a concentration in several diseases in vivo. Ergothioneine is 32 thus a potentially useful dietary supplement. Present methods of commercial production rely on 33 extraction from natural sources or on chemical synthesis. Here we describe the engineering of 34 the baker's yeast Saccharomyces cerevisiae to produce ergothioneine by fermentation in defined 35 media. After integrating combinations of ERG biosynthetic pathways from different organisms, 36 we screened yeast strains for their production of ERG. The highest-producing strain was also 37 engineered with known ergothioneine transporters. The effect of amino acid supplementation of 38 the medium was investigated and the nitrogen metabolism of S. cerevisiae was altered by knock-39 out of TOR1 or YIH1. We also optimized the media composition using fractional factorial 40 methods. Our optimal strategy led to a titer of 598 ± 18 mg/L ergothioneine in fed-batch culture 41 in bioreactors. Because S. cerevisiae is a GRAS ('generally recognised as safe') organism that is 42 2 widely used for nutraceutical production, this work provides a promising process for the 43 biosynthetic production of ERG. 44 45

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Biosynthesis of Ergothioneine and Hercynine by Fungi and Actinomycetales

Cited by 98 publications

References 13 publications

Some Prevalent Biomolecules as Defenses Against Singlet Oxygen Damage

Some Prevalent Biomolecules as Defenses Against Singlet Oxygen Damage

Mycothiol-dependent proteins in actinomycetes

Engineering the yeastSaccharomyces cerevisiaefor the production of L-(+)-ergothioneine

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