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Literature summary extracted from

  • Goncharenko, K.V.; Vit, A.; Blankenfeldt, W.; Seebeck, F.P.
    Structure of the sulfoxide synthase EgtB from the ergothioneine biosynthetic pathway (2015), Angew. Chem. Int. Ed. Engl., 54, 2821-2824.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.14.99.50 ascorbic acid required for enzyme stability Mycolicibacterium thermoresistibile

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.14.99.50 gene egtB, recombinant expression in Escherichia coli Mycolicibacterium thermoresistibile

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.14.99.50 purified recombinant enzyme, as iron-bound holoenzyme, in complex with substrate gamma-glutamyl cysteine, N-alpha-dimethyl histidine and Mn2+ or with substrate N-alpha-trimethyl histidine and Fe2+, X-ray diffraction structure determination and analysis Mycolicibacterium thermoresistibile

Protein Variants

EC Number Protein Variants Comment Organism
1.14.99.50 D416N site-directed mutagenesis, the mutation increases KM for gamma-glutamyl cysteine by 200fold but does not significantly change KM for N-alpha-trimethyl histidine or kcat compared to the wild-type enzyme Mycolicibacterium thermoresistibile

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.14.99.50 additional information
-
 additional information Michaelis-Menten kinetics Mycolicibacterium thermoresistibile

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.14.99.50 Fe2+ a non-heme iron enzyme, the two substrates and three histidine residues serve as ligands in an octahedral iron binding site, Glu140 rather than His51 is the metal ligand Mycolicibacterium thermoresistibile
1.14.99.50 Mn2+ binding structure, overview Mycolicibacterium thermoresistibile

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.14.99.50 hercynine + gamma-L-glutamyl-L-cysteine + O2 Mycolicibacterium thermoresistibile i.e. N-alpha-trimethyl histidine gamma-L-glutamyl-S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.14.99.50 Mycolicibacterium thermoresistibile G7CFI3
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.14.99.50 recombinant enzyme from Escherichia coli Mycolicibacterium thermoresistibile

Reaction

EC Number Reaction Comment Organism Reaction ID
1.14.99.50 hercynine + gamma-L-glutamyl-L-cysteine + O2 = gamma-L-glutamyl-S-(hercyn-2-yl)-L-cysteine S-oxide + H2O catalytic mechanism in which C-S bond formation is initiated by an iron(III)-complexed thiyl radical attacking the imidazole ring of N-alpha-trimethyl histidine, proposed mechanism for EgtB-catalyzed C-S bond formation and sulfoxidation, overview Mycolicibacterium thermoresistibile
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.99.50 hercynine + gamma-L-glutamyl-L-cysteine + O2 i.e. N-alpha-trimethyl histidine Mycolicibacterium thermoresistibile gamma-L-glutamyl-S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
-
 ?
1.14.99.50 hercynine + gamma-L-glutamyl-L-cysteine + O2 i.e. N-alpha-trimethyl histidine. Substrate binding mode, detailed overview Mycolicibacterium thermoresistibile gamma-L-glutamyl-S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
-
 ?
1.14.99.50 hercynine + N-glutaryl cysteine + O2 N-glutaryl cysteine is a 100fold less efficient sulfur donor for wild type EgtBthermo but a 10fold better substrate for mutant EgtBD416N than gamma-L-glutamyl-L-cysteine Mycolicibacterium thermoresistibile N-glutaryl-(hercyn-2-yl)-L-cysteine S-oxide + H2O
-
 ?

Subunits

EC Number Subunits Comment Organism
1.14.99.50 monomer the enzyme consists of an N-terminal DinB domain (residues 1-150), a two-stranded beta-sheet region (residues 151-210), and a C-terminal C-type lectin domain Mycolicibacterium thermoresistibile

Synonyms

EC Number Synonyms Comment Organism
1.14.99.50 EgtB
-
 Mycolicibacterium thermoresistibile
1.14.99.50 EgtBthermo
-
 Mycolicibacterium thermoresistibile
1.14.99.50 sulfoxide synthase
-
 Mycolicibacterium thermoresistibile

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.14.99.50 25
-
 assay at Mycolicibacterium thermoresistibile

General Information

EC Number General Information Comment Organism
1.14.99.50 evolution enzyme EgtB represents a distinct enzyme class (sulfoxide synthases) with no relation to sulfur oxidizing or C-S bond-forming iron enzymes such as cysteine dioxygenase or isopenicillin synthase Mycolicibacterium thermoresistibile
1.14.99.50 metabolism enzyme EgtB catalyzes O2-dependent C-S bond formation between gamma-glutamyl cysteine and N-alpha-trimethyl histidine as the central step in ergothioneine biosynthesis Mycolicibacterium thermoresistibile
1.14.99.50 additional information the two substrates and three histidine residues serve as ligands in an octahedral iron binding active site, enzyme structure analysis, detailed overview Mycolicibacterium thermoresistibile
1.14.99.50 physiological function enzyme EgtB catalyzes O2-dependent C-S bond formation between gamma-glutamyl cysteine and N-alpha-trimethyl histidine as the central step in ergothioneine biosynthesis Mycolicibacterium thermoresistibile