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.
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 |
|
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 |