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Literature summary extracted from

  • Wei, W.; Siegbahn, P.; Liao, R.
    Theoretical study of the mechanism of the nonheme iron enzyme EgtB (2017), Inorg. Chem., 56, 3589-3599 .
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.14.99.50 analysis of the X-ray crystal structure of EgtB from Mycobacterium thermoresistibile, solved in three different forms, namely, the apo form, in complex with iron and the N-alpha-trimethyl histidine substrate, and in complex with manganese and the two natural substrates gamma-glutamyl cysteine and alpha-trimethyl histidine at 1.98 A resolution, with the active site for the third one. X-ray structure of the active site of EgtB complex with gamma-glutamyl cysteine and N-alpha-trimethyl histidine, coordinates taken from PDB ID 4X8D. Mn is replaced by Fe in the active site Mycolicibacterium thermoresistibile

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.14.99.50 Fe2+ non-heme iron, requied for catalysis 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
-
 gamma-L-glutamyl-S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
-
 ?
1.14.99.50 hercynine + gamma-L-glutamyl-L-cysteine + O2 Mycolicibacterium thermoresistibile ATCC 19527
-
 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
-
-
1.14.99.50 Mycolicibacterium thermoresistibile ATCC 19527 G7CFI3
-
-

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 two different mechanisms are analyzed, depending on whether the sulfoxidation or the S-C bond formation takes place first. The calculations suggest that the S-O bond formation occurs first between the thiolate and the ferric superoxide, followed by homolytic O-O bond cleavage. Subsequently, proton transfer from a second-shell residue Tyr377 to the newly generated iron-oxo moiety takes place, which is followed by proton transfer from the N-alpha-trimethyl histidine imidazole to Tyr377, facilitated by two crystallographically observed water molecules. Next, the S-C bond is formed between gamma-glutamyl cysteine and N-alpha-trimethyl histidine, followed by proton transfer from the imidazole CH moiety to Tyr377, which is calculated to be the rate-limiting step for the whole reaction, with a barrier of 17.9 kcal/mol in the quintet state. Optimized structures for the second, third, and fourth steps. Detailed 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
-
 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
-
 Mycolicibacterium thermoresistibile ATCC 19527 gamma-L-glutamyl-S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.14.99.50 EgtB
-
 Mycolicibacterium thermoresistibile

General Information

EC Number General Information Comment Organism
1.14.99.50 evolution enzyme EgtB belongs to the mononuclear nonheme iron dioxygenase family Mycolicibacterium thermoresistibile
1.14.99.50 metabolism EgtB is a nonheme iron enzyme catalyzing the C-S bond formation between gamma-glutamyl cysteine and N-alpha-trimethyl histidine in the ergothioneine biosynthesis Mycolicibacterium thermoresistibile
1.14.99.50 additional information in the active site, the metal is hexacoordinated and ligated by three histidines (His51, His134, and His138), the two substrates (via a sulfide of gamma-glutamyl cysteine and an imidazole nitrogen of N-alpha-trimethyl histidine), and a water molecule. Second-shell residue, Tyr377 forms a hydrogen bond with the water molecule. In addition, two positively charged residues, Arg90 and Arg87, form hydrogen bonds with the substrate gamma-glutamyl cysteine. Several additional water molecules form a hydrogen bonding network interacting with the two substrates Mycolicibacterium thermoresistibile