EC Number   |
Protein Variants |
Reference |
|---|
   2.1.1.79 | C139S |
15% of wild-type activity |
658648 |
| 2.1.1.79 | C139S |
mutant retains 31% of the activity of the wild-type enzyme. While addition of free bicarbonate has almost no effect on the wild-type enzyme activity, the mutants enzyme is rescued by the addition of free bicarbonate. Catalytic efficiencies of the rescued mutant is 85% of wild-type activity |
678131 |
| 2.1.1.79 | C176S |
150% of wild-type activity |
658648 |
| 2.1.1.79 | C354S |
63% of wild-type activity |
658648 |
| 2.1.1.79 | E239A |
catalytic efficiency is 0.2% of wild-type value |
678131 |
| 2.1.1.79 | E239A |
mutant shows 0.57% of wild-type activity |
680343 |
| 2.1.1.79 | E239D |
mutant shows 0.96% of wild-type activity |
680343 |
| 2.1.1.79 | E239Q |
catalytic efficiency is less than 0.02% of wild-type value |
678131 |
| 2.1.1.79 | G236E |
active site mutant, replacing the strictly conserved G236 by a glutamate residue, which corresponds to E146 of the homologous mycolic acid methyltransferase. Mutant has less than 1% of the in vitro activity of the wild-type enzyme and leads to the formation of cyclopropanated fatty acid methyl esters and of new C17 methyl-branched unsaturated fatty acid methyl esters. The double bond of the latters is located at different positions 8, 9 or 10, and the methyl group at position 10 or 9. The reaction catalyzed by G236E mutant thus starts by the methylation of the unsaturated acyl chain at position 10 or 9 yielding a carbocation at position 9 or 10 respectively. It follows then two competing steps, a normal cyclopropanation or hydride shift/elimination events giving different combinations of alkenes |
733434 |
| 2.1.1.79 | G236E |
the mutant has less than 1% of the in vitro activity of the wild type enzyme. The reaction catalyzed by this G236E mutant starts by the methylation of the unsaturated acyl chain at position 10 or 9 yielding a carbocation at position 9 or 10 respectively |
733434 |
