EC Number   |
Protein Variants |
Reference |
|---|
    3.5.4.10 | K137A |
30fold increase in KM-value, 30fold decrease in kcat-value |
658026 |
| 3.5.4.10 | K137A |
dramatically reduced kcat-value |
485758 |
| 3.5.4.10 | K137R |
3fold increase in KM-value15fold decrease in kcat-value |
658026 |
| 3.5.4.10 | K137R |
dramatically reduced kcat-value |
485758 |
| 3.5.4.10 | K246R |
natural mutation observed in female infant patient with lack in transformylase activity and about 40% residual enzymic activity, showing massive excretion of 5-amino-4-imidazolecarboxamide riboside, dysmorphic features, severe neurological defects, and congenital blindness. Recombinant protein with K426R mutation completely lacks AICAR transformylase activity |
667123 |
| 3.5.4.10 | K255A |
complete loss of activity, mutation lowers the thermostability |
756701 |
| 3.5.4.10 | K255R |
mutation reduces activity by 76%. Mutation increases the Tm by approximately 3°C |
756701 |
| 3.5.4.10 | K66A |
dramatically reduced kcat-value |
485758 |
| 3.5.4.10 | K66A |
more than 100fold increase in KM-value |
658026 |
| 3.5.4.10 | N415A |
decrease in AICAR transformylase activity as compared with wild-type SlugATIC, indicating it might also play essential role in substrate binding. Increase in the thermostability |
756701 |
