Table 3. Activities of the PfTR Chimeric Mutants with Trx, Selenocystine, and Lipoic Acid.
| mol of NADPH min–1 (mol of TR)−1 |
|||||
|---|---|---|---|---|---|
| enzyme | PfTR | 90 μM Trx | 300 μM selenocystine | 5 mM lipoic acid | 50 mM H2O2 |
| PfTR-GC1GGGKC2Ga | 1 | 500 ± 20 | 410 ± 30 | 90 ± 10 | 9 ± 0.2 |
| PfTR-GC1C2Ga | 11 | 1.3 ± 0.6 | 280 ± 15 | 70 ± 2 | NDc |
| PfTR-GC1U2Gb | 12 | 1160 ± 20 | 2130 ± 60 | 255 ± 10 | 330 ± 3 |
| PfTR-GC1GGGKU2Gb | 13 | 85 ± 5 | 260 ± 15 | 145 ± 5 | 60 ± 3 |
Recombinant protein produced as a GST fusion.
Recombinant protein produced as an intein fusion via semisynthesis.
No activity detectable.