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Literature summary for 1.14.99.50 extracted from
- Convergent evolution of ergothioneine biosynthesis in cyanobacteria (2017), ChemBioChem, 18, 2115-2118 .
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| analysis of crystal structure of EgtB, PDB ID 4X8D, in complex with iron(II) and N-alpha-trimethylhistidine | Mycolicibacterium thermoresistibile |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Fe2+ | an iron-dependent sulfoxide synthase | 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 | - |
gamma-L-glutamyl-S-(hercyn-2-yl)-L-cysteine S-oxide + H2O | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Mycolicibacterium thermoresistibile | G7CFI3 | - |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| hercynine + gamma-L-glutamyl-L-cysteine + O2 | - |
Mycolicibacterium thermoresistibile | gamma-L-glutamyl-S-(hercyn-2-yl)-L-cysteine S-oxide + H2O | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| EgtB | - |
Mycolicibacterium thermoresistibile |
| sulfoxide synthase | - |
Mycolicibacterium thermoresistibile |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | Some cyanobacteria recruited and adapted a sulfoxide synthase from a different biosynthetic pathway to make ergothioneine. Evolutionary malleability of the thiohistidine biosynthetic machinery. The sulfoxide synthase EgtB catalyzes the sulfurization of N-alpha-trimethylhistidine at the imidazole 2-position and subsequent oxidation to the S-sulfoxide. The homologous sulfoxide synthases OvoA, EC 1.14.99.52, catalyze the formation of 5-histidylcysteine sulfoxide. The stereochemistry of this sulfoxide is unknown, and cyanobacterial OvoA homologues (Egt-B(ovo)) have evolved to catalyze an EgtB-type reaction by convergent evolution. Prokaryotic EgtBs are usually monofunctional, fungal EgtBs are fused to EgtD | Mycolicibacterium thermoresistibile |
| metabolism | biosynthesis of N-alpha-trimethyl-2-thiohistidine (ergothioneine) is a frequent trait in cyanobacteria. This sulfur compound may provide essential relief from oxidative stress related to oxygenic photosynthesis. The central steps in ergothioneine biosynthesis are catalyzed by a histidine methyltransferase and the iron-dependent sulfoxide synthase. Ergothioneine biosynthesis starts by trimethylation of the alpha-amino group of histidine. The resulting N-alpha-trimethylhistidine (TMH) is fused to either gamma-glutamylcysteine (in actinomycetes, EC 1.14.99.50) or cysteine (in fungi, EC 1.14.99.51). The sulfoxide product is converted into ergothoneine by removal of the glutamyl and cysteinyl moieties | Mycolicibacterium thermoresistibile |
| additional information | in a competitive reaction containing 1 mM of each histidine, N-alpha-trimethylhistidine, and cysteine, OvoAErwin produces only S-(L-histidin-5-yl)-L-cysteine S-oxide, whereas OvoAErw-NW and EgtB(ovo) produce exclusively gamma-L-glutamyl-S-(hercyn-2-yl)-L-cysteine S-oxide | Mycolicibacterium thermoresistibile |
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Release 2023.1 (January 2023)
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