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Literature summary for 1.14.99.50 extracted from
- Structure of the sulfoxide synthase EgtB from the ergothioneine biosynthetic pathway (2015), Angew. Chem. Int. Ed. Engl., 54, 2821-2824.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| ascorbic acid | required for enzyme stability | Mycolicibacterium thermoresistibile |  |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene egtB, recombinant expression in Escherichia coli | Mycolicibacterium thermoresistibile |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| 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
| Protein Variants | Comment | Organism |
|---|---|---|
| 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]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | Michaelis-Menten kinetics | Mycolicibacterium thermoresistibile |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| 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 | |
| Mn2+ | binding structure, overview | Mycolicibacterium thermoresistibile | |
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 thermoresistibile | i.e. N-alpha-trimethyl histidine | gamma-L-glutamyl-S-(hercyn-2-yl)-L-cysteine S-oxide + H2O | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Mycolicibacterium thermoresistibile | G7CFI3 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant enzyme from Escherichia coli | Mycolicibacterium thermoresistibile |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| 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)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 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 | - |
? | |
| 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 | - |
? | |
| 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
| Subunits | Comment | Organism |
|---|---|---|
| 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
| Synonyms | Comment | Organism |
|---|---|---|
| EgtB | - |
Mycolicibacterium thermoresistibile |
| EgtBthermo | - |
Mycolicibacterium thermoresistibile |
| sulfoxide synthase | - |
Mycolicibacterium thermoresistibile |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 25 | - |
assay at | Mycolicibacterium thermoresistibile |
General Information
| General Information | Comment | Organism |
|---|---|---|
| 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 |
| 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 |
| 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 |
| 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 |
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Release 2023.1 (January 2023)
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