EC Number   |
Protein Variants |
Reference |
|---|
   4.3.1.15 | C265S |
Tm-value of the mutant enzyme is 60°C, compared to 65°C for the wild-type enzyme. The activity of the C291S mutant is higher than that of C265S mutant |
748506 |
| 4.3.1.15 | C271V |
Km for DL-DAP is 47fold higher compared to wild-type and kcat decreased by 1.5fold compared to wild-type.In contrast to wild-type C271V sDAPAL exhibits only 2fold stimulation in activity even when a high concentration of KCl is used |
729923 |
| 4.3.1.15 | C271V |
mutation results in a 47fold increase in Km and 1.5fold reduction in Kcat with respect to the wild type enzyme when DL-2,3-diaminopropanoate is used as substrate |
-, 748506 |
| 4.3.1.15 | C291S |
Tm-value of the mutant enzyme is 68°C, compared to 65°C for the wild-type enzyme. The activity of the C291S mutant is higher than that of C265S mutant |
748506 |
| 4.3.1.15 | C299V |
kcat and Km for DL-DAP are similar to wild-type |
729923 |
| 4.3.1.15 | C299V |
mutation does not effect the activity |
-, 748506 |
| 4.3.1.15 | D120N |
mutant shows no reaction with D-DAP, Km (L-DAP) increased compared to wild-type, kcat decreased |
729988 |
| 4.3.1.15 | D125E |
mutant does not show any activity with D-DAP at all |
729923 |
| 4.3.1.15 | D125S |
kcat value in mutant is reduced by 5.4fold for D-DAP compared to wild-type |
729923 |
| 4.3.1.15 | D189N |
Km (D-DAP) and (L-DAP) increased compared to wild-type, kcat decreased |
729988 |
