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Literature summary extracted from
- Convergent evolution of ergothioneine biosynthesis in cyanobacteria (2017), ChemBioChem, 18, 2115-2118 .
Crystallization (Commentary)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 1.14.99.50 | analysis of crystal structure of EgtB, PDB ID 4X8D, in complex with iron(II) and N-alpha-trimethylhistidine | Mycolicibacterium thermoresistibile |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.14.99.50 | Fe2+ | an iron-dependent sulfoxide synthase | Mycolicibacterium thermoresistibile |  |
| 1.14.99.52 | Fe2+ | an iron-dependent sulfoxide synthase | Microcystis aeruginosa | |
| 1.14.99.52 | Fe2+ | an iron-dependent sulfoxide synthase | Moorena producens | |
| 1.14.99.52 | Fe2+ | an iron-dependent sulfoxide synthase | Erwinia tasmaniensis | |
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 | - |
? | |
| 1.14.99.52 | hercynine + gamma-L-glutamyl-L-cysteine + O2 | Moorena producens | - |
gamma-L-glutamyl-S-(hercyn-2-yl)-L-cysteine S-oxide + H2O | - |
? | |
| 1.14.99.52 | hercynine + gamma-L-glutamyl-L-cysteine + O2 | Moorena producens PAL-8-15-08-1 | - |
gamma-L-glutamyl-S-(hercyn-2-yl)-L-cysteine S-oxide + H2O | - |
? | |
| 1.14.99.52 | L-histidine + L-cysteine + O2 | Moorena producens | - |
S-(L-histidin-5-yl)-L-cysteine S-oxide + H2O | - |
? | |
| 1.14.99.52 | L-histidine + L-cysteine + O2 | Moorena producens PAL-8-15-08-1 | - |
S-(L-histidin-5-yl)-L-cysteine S-oxide + H2O | - |
? | |
| 1.14.99.52 | additional information | Moorena producens | an OvoA-like protein, full-length OvoA homologue, OvoA_2, is a monofunctional sulfoxide synthase | ? | - |
? | |
| 1.14.99.52 | additional information | Microcystis aeruginosa | short cyanobacterial OvoA-type enzymes may contribute to ergothioneine (EC 1.14.99.51) instead of ovothiol production | ? | - |
? | |
| 1.14.99.52 | additional information | Erwinia tasmaniensis | the ovothiol biosynthetic sulfoxide synthase OvoA from Erwinia tasmaniensis (OvoAErwin) is a promiscuous enzyme. This enzyme is most efficient in making its native product S-(L-histidin-5-yl)-L-cysteine S-oxide, but, when presented with N-alpha-trimethylhistidine as a sulfur acceptor, the enzyme switches product specificity and produces gamma-L-glutamyl-S-(hercyn-2-yl)-L-cysteine S-oxide albeit with significantly lower efficiency | ? | - |
? | |
| 1.14.99.52 | additional information | Moorena producens PAL-8-15-08-1 | an OvoA-like protein, full-length OvoA homologue, OvoA_2, is a monofunctional sulfoxide synthase | ? | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.14.99.50 | Mycolicibacterium thermoresistibile | G7CFI3 | - |
- |
| 1.14.99.52 | Erwinia tasmaniensis | - |
- |
- |
| 1.14.99.52 | Microcystis aeruginosa | - |
- |
- |
| 1.14.99.52 | Moorena producens | A0A1D8U0C7 | - |
- |
| 1.14.99.52 | Moorena producens | A0A1D8U386 | - |
- |
| 1.14.99.52 | Moorena producens PAL-8-15-08-1 | A0A1D8U0C7 | - |
- |
| 1.14.99.52 | Moorena producens PAL-8-15-08-1 | A0A1D8U386 | - |
- |
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 | - |
? | |
| 1.14.99.52 | hercynine + gamma-L-glutamyl-L-cysteine + O2 | - |
Moorena producens | gamma-L-glutamyl-S-(hercyn-2-yl)-L-cysteine S-oxide + H2O | - |
? | |
| 1.14.99.52 | hercynine + gamma-L-glutamyl-L-cysteine + O2 | - |
Moorena producens PAL-8-15-08-1 | gamma-L-glutamyl-S-(hercyn-2-yl)-L-cysteine S-oxide + H2O | - |
? | |
| 1.14.99.52 | L-histidine + L-cysteine + O2 | - |
Microcystis aeruginosa | S-(L-histidin-5-yl)-L-cysteine S-oxide + H2O | - |
? | |
| 1.14.99.52 | L-histidine + L-cysteine + O2 | - |
Moorena producens | S-(L-histidin-5-yl)-L-cysteine S-oxide + H2O | - |
? | |
| 1.14.99.52 | L-histidine + L-cysteine + O2 | - |
Erwinia tasmaniensis | S-(L-histidin-5-yl)-L-cysteine S-oxide + H2O | - |
? | |
| 1.14.99.52 | L-histidine + L-cysteine + O2 | - |
Moorena producens PAL-8-15-08-1 | S-(L-histidin-5-yl)-L-cysteine S-oxide + H2O | - |
? | |
| 1.14.99.52 | additional information | an OvoA-like protein, full-length OvoA homologue, OvoA_2, is a monofunctional sulfoxide synthase | Moorena producens | ? | - |
? | |
| 1.14.99.52 | additional information | short cyanobacterial OvoA-type enzymes may contribute to ergothioneine (EC 1.14.99.51) instead of ovothiol production | Microcystis aeruginosa | ? | - |
? | |
| 1.14.99.52 | additional information | the ovothiol biosynthetic sulfoxide synthase OvoA from Erwinia tasmaniensis (OvoAErwin) is a promiscuous enzyme. This enzyme is most efficient in making its native product S-(L-histidin-5-yl)-L-cysteine S-oxide, but, when presented with N-alpha-trimethylhistidine as a sulfur acceptor, the enzyme switches product specificity and produces gamma-L-glutamyl-S-(hercyn-2-yl)-L-cysteine S-oxide albeit with significantly lower efficiency | Erwinia tasmaniensis | ? | - |
? | |
| 1.14.99.52 | 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 | Moorena producens | ? | - |
? | |
| 1.14.99.52 | additional information | an OvoA-like protein, full-length OvoA homologue, OvoA_2, is a monofunctional sulfoxide synthase | Moorena producens PAL-8-15-08-1 | ? | - |
? | |
| 1.14.99.52 | 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 | Moorena producens PAL-8-15-08-1 | ? | - |
? | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.14.99.50 | EgtB | - |
Mycolicibacterium thermoresistibile |
| 1.14.99.50 | sulfoxide synthase | - |
Mycolicibacterium thermoresistibile |
| 1.14.99.52 | OvoA | - |
Moorena producens |
| 1.14.99.52 | OvoA-like protein | - |
Microcystis aeruginosa |
| 1.14.99.52 | OvoA-like protein | - |
Moorena producens |
| 1.14.99.52 | OvoAErwin | - |
Erwinia tasmaniensis |
| 1.14.99.52 | OvoA_1 | - |
Moorena producens |
| 1.14.99.52 | OvoA_2 | - |
Moorena producens |
| 1.14.99.52 | short OvoA homologue | - |
Microcystis aeruginosa |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 1.14.99.50 | 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 |
| 1.14.99.50 | 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 |
| 1.14.99.50 | 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 |
| 1.14.99.52 | evolution | cyanobacterial OvoA homologues (Egt-B(ovo)) have evolved to catalyze an EgtB-type reaction by convergent evolution, cf. EC 1.14.99.50, in a competitive reaction containing 1 mM of each histidine, N-alpha-trimethylhistidine, and cysteine, OvoAErw-NW and EgtB(ovo) produce exclusively gamma-L-glutamyl-S-(hercyn-2-yl)-L-cysteine S-oxide | Microcystis aeruginosa |
| 1.14.99.52 | evolution | cyanobacterial OvoA homologues (Egt-B(ovo)) have evolved to catalyze an EgtB-type reaction by convergent evolution, cf. EC 1.14.99.50, in a competitive reaction containing 1 mM of each histidine, N-alpha-trimethylhistidine, and cysteine, OvoAErw-NW and EgtB(ovo) produce exclusively gamma-L-glutamyl-S-(hercyn-2-yl)-L-cysteine S-oxide | Moorena producens |
| 1.14.99.52 | evolution | cyanobacterial OvoA homologues (Egt-B(ovo)) have evolved to catalyze an EgtB-type reaction by convergent evolution, cf. EC 1.14.99.50, in a competitive reaction containing 1 mM of each histidine, N-alpha-trimethylhistidine, and cysteine, OvoAErw-NW and EgtB(ovo) produce exclusively gamma-L-glutamyl-S-(hercyn-2-yl)-L-cysteine S-oxide. Because Erwinia tasmaniensis and most other OvoA encoding organisms do not encode an EgtD-type histidine methyltransferase, it seems clear that this N-alpha-trimethylhistidine-consuming side activity of OvoAErwin has no physiological purpose. Such promiscuity may have facilitated the transition of an ancestral sulfoxide synthase from ovothiol to erothioneine biosynthesis | Erwinia tasmaniensis |
| 1.14.99.52 | metabolism | sulfoxide synthase OvoA catalyzes the formation of 5-histidylcysteine sulfoxide in the ovothiol biosynthesis. Short cyanobacterial OvoA-type enzymes may contribute to ergothioneine (EC 1.14.99.51) instead of ovothiol production | Microcystis aeruginosa |
| 1.14.99.52 | metabolism | sulfoxide synthase OvoA catalyzes the formation of 5-histidylcysteine sulfoxide in the ovothiol biosynthesis. Short cyanobacterial OvoA-type enzymes may contribute to ergothioneine (EC 1.14.99.51) instead of ovothiol production | Moorena producens |
| 1.14.99.52 | metabolism | sulfoxide synthase OvoA catalyzes the formation of 5-histidylcysteine sulfoxide in the ovothiol biosynthesis. Short cyanobacterial OvoA-type enzymes may contribute to ergothioneine (EC 1.14.99.51) instead of ovothiol production | Erwinia tasmaniensis |
| 1.14.99.52 | additional information | an OvoA-like protein, full-length OvoA homologue, OvoA_1, with a C-terminal methyltransferase, most OvoAs contain a C-terminal methyltransferase | Moorena producens |
| 1.14.99.52 | additional information | homologue OvoA_2 is a monofunctional sulfoxide synthase without a C-terminal methyltransferase | Moorena producens |
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