EC Number   |
Protein Variants |
Reference |
|---|
   1.14.99.50 | A420Y |
position is involved in controlling the reaction selectiviy. Mutant leads to an increased amount of side-reaction (cysteine dioxygenase activity) |
763798 |
| 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 |
733092 |
| 1.14.99.50 | D52L |
mutation may disrupt the hydrogen bond between Asp52 and glutamyl group of substrate gamma-Glu-Cys, which in turn alters the substrate selectivity |
763798 |
| 1.14.99.50 | D52L/A420Y |
mutation tunes EgtB activity toward Egt1-type, i.e. reaction of EC 1.21.3.10 |
763798 |
| 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 |
744679 |
| 1.14.99.50 | Y377F |
site-directed mutagenesis, the single point mutation in EgtB completely uncouples substrate consumption from sulfoxide synthase activity with the native substrates hercynine and gamma-glutamyl cysteine, with EgtB exclusively oxidizing gamma-glutamyl cysteine to the sulfinic acid. Tyr377 is hydrogen bonded to a water molecule that coordinates to the iron |
745390 |
