EC Number   |
Protein Variants |
Reference |
|---|
   1.18.1.5 | C73G |
surface mutation facilitating crystallization without affecting cluster ligation and with only minor effects on activity |
717023 |
| 1.18.1.5 | C73S |
mutation improves protein stability. Decreasing order of stability is C73S/C85S, C73S, C85S, wild-type Pdx |
717987 |
| 1.18.1.5 | C73S/C85S |
mutation improves protein stability. Decreasing order of stability is C73S/C85S, C73S, C85S, wild-type Pdx |
717987 |
| 1.18.1.5 | C85S |
mutation improves protein stability. Decreasing order of stability is C73S/C85S, C73S, C85S, wild-type Pdx |
717987 |
| 1.18.1.5 | D38A |
mutation does not affect assembly of the [2Fe-2S] cluster and results in a marginal change in the redox potential of Pdx. 45% of wild-type activity |
717770 |
| 1.18.1.5 | D38N |
mutation does not affect assembly of the [2Fe-2S] cluster and results in a marginal change in the redox potential of Pdx. 33% of wild-type activity |
717770 |
| 1.18.1.5 | K339A |
moderate decrease in the binding affinity and reduction of Pdx |
717247 |
| 1.18.1.5 | K387A |
moderate decrease in the binding affinity and reduction of Pdx |
717247 |
| 1.18.1.5 | K409A |
moderate decrease in the binding affinity and reduction of Pdx |
717247 |
| 1.18.1.5 | more |
expression of wild-type as His-tagged protein. Molecular, spectral, and electron transferring properties of recombinant His6-Pdr to artificial and native electron acceptors are similar to those of the wild-type protein. Contrary to wild-type, under anaerobic conditions, NAD+ induces in His6 Pdr spectral changes indicative of flavin reduction and formation of the charge transfer complex between the reduced FAD and NAD+ |
717764 |
