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IUBMB CommentsContains pyridoxal 5'-phosphate. The enzyme, characterized from the bacterium Mycobacterium smegmatis, cayalyses the last step in the pathway of ergothioneine biosynthesis. The enzyme forms a 2-(hydroxysulfanyl)hercynine intermediate, which is reduced to ergothioneine non-enzymically by a thiol. In vitro, DTT can serve this function.
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(2R)-3-(2-[[(2R)-2-amino-2-carboxyethyl]sulfanyl]-2,3-dihydro-1H-imidazol-4-yl)-2-(trimethylazaniumyl)propanoate + reduced acceptor
(2R)-3-(2-sulfido-2,3-dihydro-1H-imidazol-4-yl)-2-(trimethylazaniumyl)propanoate + pyruvate + ammonia + acceptor
thioether variant of S-(hercyn-2-yl)-L-cysteine S-oxide
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2-(hydroxysulfanyl)hercynine + reduced acceptor
ergothioneine + acceptor + H2O
S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
2-(hydroxysulfanyl)hercynine + pyruvate + ammonia
S-(hercyn-2-yl)-L-cysteine S-oxide + reduced acceptor
ergothioneine + pyruvate + ammonia + acceptor
additional information
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2-(hydroxysulfanyl)hercynine + reduced acceptor
ergothioneine + acceptor + H2O
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2-(hydroxysulfanyl)hercynine + reduced acceptor
ergothioneine + acceptor + H2O
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2-(hydroxysulfanyl)hercynine + reduced acceptor
ergothioneine + acceptor + H2O
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2-(hydroxysulfanyl)hercynine + reduced acceptor
ergothioneine + acceptor + H2O
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S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
2-(hydroxysulfanyl)hercynine + pyruvate + ammonia
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S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
2-(hydroxysulfanyl)hercynine + pyruvate + ammonia
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S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
2-(hydroxysulfanyl)hercynine + pyruvate + ammonia
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S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
2-(hydroxysulfanyl)hercynine + pyruvate + ammonia
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S-(hercyn-2-yl)-L-cysteine S-oxide + reduced acceptor
ergothioneine + pyruvate + ammonia + acceptor
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S-(hercyn-2-yl)-L-cysteine S-oxide + reduced acceptor
ergothioneine + pyruvate + ammonia + acceptor
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S-(hercyn-2-yl)-L-cysteine S-oxide + reduced acceptor
ergothioneine + pyruvate + ammonia + acceptor
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S-(hercyn-2-yl)-L-cysteine S-oxide + reduced acceptor
ergothioneine + pyruvate + ammonia + acceptor
overall reaction
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S-(hercyn-2-yl)-L-cysteine S-oxide + reduced acceptor
ergothioneine + pyruvate + ammonia + acceptor
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S-(hercyn-2-yl)-L-cysteine S-oxide + reduced acceptor
ergothioneine + pyruvate + ammonia + acceptor
overall reaction
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S-(hercyn-2-yl)-L-cysteine S-oxide + reduced acceptor
ergothioneine + pyruvate + ammonia + acceptor
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S-(hercyn-2-yl)-L-cysteine S-oxide + reduced acceptor
ergothioneine + pyruvate + ammonia + acceptor
overall reaction
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S-(hercyn-2-yl)-L-cysteine S-oxide + reduced acceptor
ergothioneine + pyruvate + ammonia + acceptor
overall reaction
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S-(hercyn-2-yl)-L-cysteine S-oxide + reduced acceptor
ergothioneine + pyruvate + ammonia + acceptor
overall reaction
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additional information
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S-(hercyn-2-yl)-L-cysteine S-oxide is the native EgtE substrate and a sulfenic acid intermediate is involved in the ergothioneine C-S lyase reaction
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additional information
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enzyme activity determination by a 1H NMR assay of chemical shift of the imidazole hydrogen atoms and a colorimetric assay by coupling the C-S lyase reaction with lactate dehydrogenas, product determination by high-resolution mass spectrometry and NMR
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additional information
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enzyme activity determination by a 1H NMR assay of chemical shift of the imidazole hydrogen atoms and a colorimetric assay by coupling the C-S lyase reaction with lactate dehydrogenas, product determination by high-resolution mass spectrometry and NMR
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additional information
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enzyme activity determination by a 1H NMR assay of chemical shift of the imidazole hydrogen atoms and a colorimetric assay by coupling the C-S lyase reaction with lactate dehydrogenas, product determination by high-resolution mass spectrometry and NMR
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additional information
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the ergothioneine pathway can also synthesize selenoneine, a selenium-containing derivative of ergothioneine, when the culture medium is supplemented with selenium. Selenoneine biosynthesis, unlike ergothioneine biosynthesis, does not produce a sulfoxide as its intermediate, but produces hercynylselenocysteine instead
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additional information
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the ergothioneine pathway can also synthesize selenoneine, a selenium-containing derivative of ergothioneine, when the culture medium is supplemented with selenium. Selenoneine biosynthesis, unlike ergothioneine biosynthesis, does not produce a sulfoxide as its intermediate, but produces hercynylselenocysteine instead
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2-(hydroxysulfanyl)hercynine + reduced acceptor
ergothioneine + acceptor + H2O
S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
2-(hydroxysulfanyl)hercynine + pyruvate + ammonia
S-(hercyn-2-yl)-L-cysteine S-oxide + reduced acceptor
ergothioneine + pyruvate + ammonia + acceptor
additional information
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2-(hydroxysulfanyl)hercynine + reduced acceptor
ergothioneine + acceptor + H2O
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2-(hydroxysulfanyl)hercynine + reduced acceptor
ergothioneine + acceptor + H2O
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2-(hydroxysulfanyl)hercynine + reduced acceptor
ergothioneine + acceptor + H2O
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S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
2-(hydroxysulfanyl)hercynine + pyruvate + ammonia
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S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
2-(hydroxysulfanyl)hercynine + pyruvate + ammonia
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S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
2-(hydroxysulfanyl)hercynine + pyruvate + ammonia
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S-(hercyn-2-yl)-L-cysteine S-oxide + reduced acceptor
ergothioneine + pyruvate + ammonia + acceptor
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S-(hercyn-2-yl)-L-cysteine S-oxide + reduced acceptor
ergothioneine + pyruvate + ammonia + acceptor
overall reaction
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S-(hercyn-2-yl)-L-cysteine S-oxide + reduced acceptor
ergothioneine + pyruvate + ammonia + acceptor
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S-(hercyn-2-yl)-L-cysteine S-oxide + reduced acceptor
ergothioneine + pyruvate + ammonia + acceptor
overall reaction
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S-(hercyn-2-yl)-L-cysteine S-oxide + reduced acceptor
ergothioneine + pyruvate + ammonia + acceptor
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S-(hercyn-2-yl)-L-cysteine S-oxide + reduced acceptor
ergothioneine + pyruvate + ammonia + acceptor
overall reaction
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S-(hercyn-2-yl)-L-cysteine S-oxide + reduced acceptor
ergothioneine + pyruvate + ammonia + acceptor
overall reaction
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S-(hercyn-2-yl)-L-cysteine S-oxide + reduced acceptor
ergothioneine + pyruvate + ammonia + acceptor
overall reaction
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additional information
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the ergothioneine pathway can also synthesize selenoneine, a selenium-containing derivative of ergothioneine, when the culture medium is supplemented with selenium. Selenoneine biosynthesis, unlike ergothioneine biosynthesis, does not produce a sulfoxide as its intermediate, but produces hercynylselenocysteine instead
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?
additional information
?
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the ergothioneine pathway can also synthesize selenoneine, a selenium-containing derivative of ergothioneine, when the culture medium is supplemented with selenium. Selenoneine biosynthesis, unlike ergothioneine biosynthesis, does not produce a sulfoxide as its intermediate, but produces hercynylselenocysteine instead
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1.96
(2R)-3-(2-[[(2R)-2-amino-2-carboxyethyl]sulfanyl]-2,3-dihydro-1H-imidazol-4-yl)-2-(trimethylazaniumyl)propanoate
pH 8.0, temperature not specified in the publication
0.121 - 0.195
S-(hercyn-2-yl)-L-cysteine S-oxide
0.121
S-(hercyn-2-yl)-L-cysteine S-oxide
pH 8.0, temperature not specified in the publication
0.1947
S-(hercyn-2-yl)-L-cysteine S-oxide
pH and temperature not specified in the publication
0.195
S-(hercyn-2-yl)-L-cysteine S-oxide
pH not specified in the publication, temperature not specified in the publication
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metabolism
SPBC660.12c locus egt2+ represents the gene primarily responsible for the second step of ergothioneine biosynthesis in Schizosaccharomyces pombe
metabolism
the enzyme catalyzes a pyridoxal 5'-phosphate-mediated C-S lyase reaction in the ergothioneine biosynthesis
metabolism
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SPBC660.12c locus egt2+ represents the gene primarily responsible for the second step of ergothioneine biosynthesis in Schizosaccharomyces pombe
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metabolism
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the enzyme catalyzes a pyridoxal 5'-phosphate-mediated C-S lyase reaction in the ergothioneine biosynthesis
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metabolism
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the enzyme catalyzes a pyridoxal 5'-phosphate-mediated C-S lyase reaction in the ergothioneine biosynthesis
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physiological function
a gene deletion mutant shows a substantial decrease in ergothioneine, accompanied by accumulation of its immediate precursor, hercynylcysteine sulfoxide. Ergothioneine-deficient strains exhibit no phenotypic defects during vegetative growth or quiescence. The ergothioneine pathway can also synthesize selenoneine, a selenium-containing derivative of ergothioneine, when the culture medium is supplemented with selenium
physiological function
gene cluster egtABCDE is responsible for biosynthesis of ergothioneine. The final reaction, conversion of S-(hercyn-2-yl)-L-cysteine S-oxide into ergothioneine, is catalyzed by EgtE
physiological function
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a gene deletion mutant shows a substantial decrease in ergothioneine, accompanied by accumulation of its immediate precursor, hercynylcysteine sulfoxide. Ergothioneine-deficient strains exhibit no phenotypic defects during vegetative growth or quiescence. The ergothioneine pathway can also synthesize selenoneine, a selenium-containing derivative of ergothioneine, when the culture medium is supplemented with selenium
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physiological function
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gene cluster egtABCDE is responsible for biosynthesis of ergothioneine. The final reaction, conversion of S-(hercyn-2-yl)-L-cysteine S-oxide into ergothioneine, is catalyzed by EgtE
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additional information
construction of an egt2+ overexpression system by replacing its native promoter with the nmt1+ promoter, which is inducible in the absence of thiamine. Generation of a egt2+ deletion mutant, DELTAegt2, by replacing the target loci in the wild-type 972 strain with the kanamycin resistance marker (kanMX). Mutant DELTASPBC660.12c, designated DELTAegt2, shows a substantial decrease in ergothioneine, accompanied by accumulation of its immediate precursor, hercynylcysteine sulfoxide. Ergothioneine-deficient strains exhibit no phenotypic defects during vegetative growth or quiescence. Construction of multiple deletion mutants of SPBC660.12c (egt2+) with the other candidate EgtE homologues, but even in successfully constructed double and triple mutants, a significant amount of EGT still remains, because hercynylcysteine sulfoxide can spontaneously convert into ergothioneine in the presence of pyridoxal 5'phosphate. Mutant DELTAegt1 strain shows no growth defects during cultivation in either rich (YE) or minimal (EMM2) culture media, deletion of gene egt1+ causes no significant perturbation to the intracellular metabolome of quiescent cells
additional information
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construction of an egt2+ overexpression system by replacing its native promoter with the nmt1+ promoter, which is inducible in the absence of thiamine. Generation of a egt2+ deletion mutant, DELTAegt2, by replacing the target loci in the wild-type 972 strain with the kanamycin resistance marker (kanMX). Mutant DELTASPBC660.12c, designated DELTAegt2, shows a substantial decrease in ergothioneine, accompanied by accumulation of its immediate precursor, hercynylcysteine sulfoxide. Ergothioneine-deficient strains exhibit no phenotypic defects during vegetative growth or quiescence. Construction of multiple deletion mutants of SPBC660.12c (egt2+) with the other candidate EgtE homologues, but even in successfully constructed double and triple mutants, a significant amount of EGT still remains, because hercynylcysteine sulfoxide can spontaneously convert into ergothioneine in the presence of pyridoxal 5'phosphate. Mutant DELTAegt1 strain shows no growth defects during cultivation in either rich (YE) or minimal (EMM2) culture media, deletion of gene egt1+ causes no significant perturbation to the intracellular metabolome of quiescent cells
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Seebeck, F.P.
In vitro reconstitution of Mycobacterial ergothioneine biosynthesis
J. Am. Chem. Soc.
132
6632-6633
2010
Neurospora crassa (A7UX13), Neurospora crassa DSM 1257 (A7UX13)
brenda
Khonde, P.L.; Jardine, A.
Improved synthesis of the super antioxidant, ergothioneine, and its biosynthetic pathway intermediates
Org. Biomol. Chem.
13
1415-1419
2015
Mycolicibacterium smegmatis
brenda
Hu, W.; Song, H.; Sae Her, A.; Bak, D.W.; Naowarojna, N.; Elliott, S.J.; Qin, L.; Chen, X.; Liu, P.
Bioinformatic and biochemical characterizations of C-S bond formation and cleavage enzymes in the fungus Neurospora crassa ergothioneine biosynthetic pathway
Org. Lett.
16
5382-5385
2014
Neurospora crassa (A7UX13), Neurospora crassa DSM 1257 (A7UX13), Neurospora crassa ATCC 24698 (A7UX13)
brenda
Pluskal, T.; Ueno, M.; Yanagida, M.
Genetic and metabolomic dissection of the ergothioneine and selenoneine biosynthetic pathway in the fission yeast, S. pombe, and construction of an overproduction system
PLoS ONE
9
e97774
2014
Schizosaccharomyces pombe (O94431), Schizosaccharomyces pombe 972 (O94431)
brenda
Song, H.; Hu, W.; Naowarojna, N.; Her, A.S.; Wang, S.; Desai, R.; Qin, L.; Chen, X.; Liu, P.
Mechanistic studies of a novel C-S lyase in ergothioneine biosynthesis the involvement of a sulfenic acid intermediate
Sci. Rep.
5
11870
2015
Mycolicibacterium smegmatis (A0R5M7)
brenda