EC Number   |
Protein Variants |
Reference |
|---|
   1.20.1.1 | E175A |
the mutation allows the enzyme to use both NAD+ and NADP+ |
-, 744691 |
| 1.20.1.1 | E175A/A176R |
double mutant, 3.6-fold higher efficiency with NAD+, 1000-fold higher efficiency with NADP+, 3-fold favor for NADP+ over NAD+ as cofactor |
-, 657956, 658259 |
| 1.20.1.1 | E175A/A176R |
mutant utilizes both NAD+ and NADP+, kinetic isotope effects study, hydride transfer step is partially rate determining |
673526 |
| 1.20.1.1 | E266Q |
higher activity, steady-state and pre-steady-state rates are comparable |
-, 690884 |
| 1.20.1.1 | E266Q |
significant increase in Km for both substrates, increase in turnover |
-, 658120 |
| 1.20.1.1 | E332N |
increases solubility and activity, thermostability almost identical to that of the wild-type enzyme |
691424 |
| 1.20.1.1 | F198I |
leads to low activity |
691424 |
| 1.20.1.1 | F198M |
increases the half-life of thermal inactivation at 45°C from around 1 min to 2 min |
691424 |
| 1.20.1.1 | H292F |
almost complete loss of activity |
658120 |
| 1.20.1.1 | H292F |
no activity, NAD+ binding is abolished |
-, 658259 |
