EC Number   |
Protein Variants |
Reference |
|---|
   5.1.3.31 | C66S |
site-directed mutagenesis, the enzyme mutant recognizes deoxy sugars as substrates. In PcDTE_C66S/deoxy sugar complex structures, bound ligand molecules in both the linear and ring forms are detected in the hydrophobic groove, while bound ligand molecules in the catalytic site are in the linear form |
746850 |
| 5.1.3.31 | R118W |
site-directed mutagenesis, the unique hydrogen bond between Arg118 and O4 of D-fructose is broken when Arg118 is mutated to Trp, the mutation improves the substrate recognition and activity of the enzyme. The mutant enzyme RsDTE_R118W shows decreased catalytic activity compared to the wild-type enzyme toward D-fructose, the kcat/Km for D-tagatose is about twofold higher than for D-psicose. Mutant R118W shows 1.5fold higher catalytic efficiency toward D-tagatose than the wild-type |
-, 748592 |
| 5.1.3.31 | Y39A |
the Vmax value of the mutant is about one-half of the Vmax value of the wild-type enzyme. The Km values for L-ribulose of the mutant and wild-type enzymes did not differ greatly |
726587 |
