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Literature summary for 1.14.99.50 extracted from

  • 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 (2014), Org. Lett., 16, 5382-5385.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.14.99.50

Cloned(Commentary)

Cloned (Comment) Organism
recombinant overexpression of Strep-tagged enzyme in Escherichia coli Mycolicibacterium smegmatis

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ a mononuclear non-heme iron enzyme Mycolicibacterium smegmatis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
hercynine + gamma-L-glutamyl-L-cysteine + O2 Mycolicibacterium smegmatis
-
 gamma-L-glutamyl-S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
-
 ?
hercynine + gamma-L-glutamyl-L-cysteine + O2 Mycolicibacterium smegmatis the enzyme is extremely specific in terms of substrate specificity gamma-L-glutamyl-S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
-
 ?
hercynine + gamma-L-glutamyl-L-cysteine + O2 Mycolicibacterium smegmatis ATCC 700084
-
 gamma-L-glutamyl-S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
-
 ?
hercynine + gamma-L-glutamyl-L-cysteine + O2 Mycolicibacterium smegmatis ATCC 700084 the enzyme is extremely specific in terms of substrate specificity gamma-L-glutamyl-S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
-
 ?

Organism

Organism UniProt Comment Textmining
Mycolicibacterium smegmatis A0R5N0 gene egtB
-
Mycolicibacterium smegmatis ATCC 700084 A0R5N0 gene egtB
-

Purification (Commentary)

Purification (Comment) Organism
recombinant Strep-tagged enzyme from Escherichia coli by affinity chromatography Mycolicibacterium smegmatis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
hercynine + gamma-L-glutamyl-L-cysteine + O2
-
 Mycolicibacterium smegmatis gamma-L-glutamyl-S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
-
 ?
hercynine + gamma-L-glutamyl-L-cysteine + O2 the enzyme is extremely specific in terms of substrate specificity Mycolicibacterium smegmatis gamma-L-glutamyl-S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
-
 ?
hercynine + gamma-L-glutamyl-L-cysteine + O2
-
 Mycolicibacterium smegmatis ATCC 700084 gamma-L-glutamyl-S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
-
 ?
hercynine + gamma-L-glutamyl-L-cysteine + O2 the enzyme is extremely specific in terms of substrate specificity Mycolicibacterium smegmatis ATCC 700084 gamma-L-glutamyl-S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
-
 ?

Synonyms

Synonyms Comment Organism
EgtB
-
 Mycolicibacterium smegmatis

General Information

General Information Comment Organism
evolution the two known sulfoxide synthases EgtB and OvoA distinguish themselves from each other by their substrate preferences and product C-S bond regioselectivity Mycolicibacterium smegmatis
metabolism the enzyme catalyzes a step in the ergothioneine biosynthetic pathway, overview Mycolicibacterium smegmatis
metabolism the enzyme is involved in the ergothioneine biosynthesis catalyzing a direct four-electron oxidative process, coupling between hercynine and gamma-L-glutamyl-L-cysteine, overview Mycolicibacterium smegmatis