EC Number   |
Protein Variants |
Reference |
|---|
    4.2.1.42 | H328A |
inactive. Mutation totally eliminates both the dehydration and epimerization activities using both L-talarate and galactarate |
-, 678325 |
| 4.2.1.42 | H328N |
inactive. Mutation totally eliminates both the dehydration and epimerization activities using both L-talarate and galactarate |
-, 678325 |
| 4.2.1.42 | H45Q |
has no detectable activity |
702265 |
| 4.2.1.42 | K197A |
inactive mutant enzyme, the structure of the K197A mutant enzyme complexed with Mg2+ and L-glucarate is determined by molecular replacement using the SeMet-substituted STM3697 structure as the search model |
678325 |
| 4.2.1.42 | K197A |
inactive. Mutation totally eliminates both the dehydration and epimerization activities using both L-talarate and galactarate |
-, 678325 |
| 4.2.1.42 | R162N |
retains a small amount of activity |
702265 |
| 4.2.1.42 | Y164F |
has no detectable activity |
702265 |
| 4.2.1.42 | Y90F |
is catalytically impaired. Structure of the mutant in complex with Mg2+ and galactarate has a well-defined C-terminal segment through residue 387, well-ordered electron density for galactarate, and Mg2+ ions in both metal sites for both protomers comprising the asymmetric unit |
702265 |
