Protein Variants | Comment | Organism |
---|---|---|
I135F/C176Y/V245F/L246I/Y273F | four out of five mutations are located in the tunnels and introduce bulkier residues, which narrowed the p1 and p2 tunnels leading to its active site. The mutant enzyme has higher activity toward 1,2,3-trichloropropane than the wild-type, with enhancements of 32fold on the catalytic constant kcat and 26fold on the catalytic efficiency (kcat/Km). The carbon-halogen bond is the rate-limiting step in the wild-type. This step is enhanced in DhaA31 due to a significantly higher number of reactive configurations of the substrate and a decrease of the energy barrier to the SN2 reaction. C176Y and V245F are identified as the key mutations responsible for most of those improvements. The release of the alcohol product is the rate-limiting step in the mutant enzyme primarily due to the C176Y mutation. Mutational dissection of the mutant and kinetic analysis of the intermediate mutants confirm the theoretical observations | Rhodococcus rhodochrous |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Rhodococcus rhodochrous | P0A3G2 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
1,2,3-trichloropropane + H2O | 1,2,3-trichloropropane is a persistent anthropogenic toxic pollutant that can be converted to the less toxic 2,3-dichloropropan-1-ol | Rhodococcus rhodochrous | 2,3-dichloropropan-1-ol + chloride | - |
? |
Synonyms | Comment | Organism |
---|---|---|
DhaA | - |
Rhodococcus rhodochrous |