EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
1.14.99.50 | Y377F | site-directed mutagenesis, the mutation results in conversion of the non-heme iron-dependent sulfoxide synthase into a thiol dioxygenase, purified enzyme mutant EgtBY377F contains 0.64% equiv. of iron as inferred by a ferrozine-based colorimetric assay, and shows reduced activity compared to the wild-type enzyme | Mycolicibacterium thermoresistibile |
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 | |
1.14.99.50 | 0.012 | - |
hercynine | pH 8.0, 26°C, recombinant enzyme mutant Y377F | Mycolicibacterium thermoresistibile | |
1.14.99.50 | 0.022 | - |
hercynine | pH 6.0, 26°C, recombinant enzyme mutant Y377F | Mycolicibacterium thermoresistibile |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
1.14.99.50 | Fe2+ | the enzyme is a non-heme iron-dependent sulfoxide synthase | Mycolicibacterium thermoresistibile |
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 | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.14.99.50 | Mycolicibacterium thermoresistibile | G7CFI3 | - |
- |
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 | additional information | product formation is monitored by cation exchange HPLC using 20 mM phosphoric acid at pH 2 as a mobile phase, and EgtB substrates and products are quantified by 1H NMR, overview | Mycolicibacterium thermoresistibile | ? | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
1.14.99.50 | ? | x * 31600, about, wild-type and mutant enzymes, mass spectrometry | Mycolicibacterium thermoresistibile |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.14.99.50 | EgtB | - |
Mycolicibacterium thermoresistibile |
EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.14.99.50 | 0.85 | - |
hercynine | pH 8.0, 26°C, recombinant enzyme mutant Y377F | Mycolicibacterium thermoresistibile | |
1.14.99.50 | 1.2 | - |
hercynine | pH 6.0, 26°C, recombinant enzyme mutant Y377F | Mycolicibacterium thermoresistibile |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
1.14.99.50 | 6 | 8 | assay at, pH 8.0 results in higher catalytic efficiency | Mycolicibacterium thermoresistibile |
EC Number | General Information | Comment | Organism |
---|---|---|---|
1.14.99.50 | malfunction | a single point mutation Y377F converts this enzyme into a gamma-glutamyl cysteine dioxygenase with an efficiency that rivals naturally evolved thiol dioxygenases | Mycolicibacterium thermoresistibile |
1.14.99.50 | physiological function | EgtB from Mycobacterium thermoresistibile catalyzes O2-dependent sulfur-carbon bond formation between the side chains of Nalpha-trimethyl histidine and gamma-glutamyl cysteine as a central step in ergothioneine biosynthesis | Mycolicibacterium thermoresistibile |
EC Number | kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.14.99.50 | 57 | - |
hercynine | pH 6.0, 26°C, recombinant enzyme mutant Y377F | Mycolicibacterium thermoresistibile | |
1.14.99.50 | 74 | - |
hercynine | pH 8.0, 26°C, recombinant enzyme mutant Y377F | Mycolicibacterium thermoresistibile |