EC Number   |
Protein Variants |
Reference |
|---|
    2.3.1.87 | C177A |
fully active, not sensitive to oxidation or N-ethylmaleimide |
487641 |
| 2.3.1.87 | C61A |
fully active, not sensitive to oxidation or N-ethylmaleimide |
487641 |
| 2.3.1.87 | E26A |
22-32fold decrease in the kcat relative to that of the wild type, catalytic efficiency is less than 10% of wild-type. Residue E26 is the general base in catalysis |
735681 |
| 2.3.1.87 | H120Q |
crystallographic studies, role in enzymic reaction |
487642 |
| 2.3.1.87 | H122Q |
crystallographic studies, role in enzymic reaction |
487642 |
| 2.3.1.87 | H122Q/H120Q |
crystallographic studies, role in enzymic reaction |
487642 |
| 2.3.1.87 | H206A |
3-4-old decrease in the kcat and an increase in the Km for both acetyl-CoA (7fold) and histamine (4fold) |
735681 |
| 2.3.1.87 | H28Y |
H28Y mutation in NAT is the cause of reduced NAT levels in vivo |
675629 |
| 2.3.1.87 | I57A/V59A |
site-directed mutagenesis, the mutant shows reduced enzyme activity and altered inhibitor binding compared to the wild-type enzyme |
704421 |
| 2.3.1.87 | more |
AANAT2 diversification is limited by stabilizing selection conferring to the enzyme well conserved secondary and tertiary structures. Only a few changes in amino acids appeared sufficient to induce different enzyme activity patterns |
720470 |
