EC Number   |
Protein Variants |
Reference |
|---|
   2.3.1.255 | S39P |
site-directed mutagenesis, the mutation does not cause a phenotype |
-, 756675 |
| 2.3.1.255 | T105A |
the mutant shows 3fold increase in Km, with no significant difference in kcat compared to the wild type enzyme |
730955 |
| 2.3.1.255 | T406Y |
site-directed mutagenesis, the hNAA15-T406Y-V5 hNatA mutant complex displays a decreased catalytic activity toward the hNatA substrate SESS compared to wild-type hNatA. the hNAA15 mutant can disassociate hNAA50 from hNatA in vitro, hNAA10 binding is not affected |
757754 |
| 2.3.1.255 | V107F |
site-directed mutagenesis, the mutation leads to a reduction in catalytic activity for the peptide substrates EEEI and SESS by 95% compared to wild-type |
756675 |
| 2.3.1.255 | V111G |
a naturally occuring 332 T > G missense mutant, the mutant Naa10 has a reduced stability and 85% reduced monomeric catalytic activity, while catalytic NatA function remains unaltered. NAA10-V111G has a reduced stability compared to wild-type NAA10, and in vitro acetylation assays reveal a reduced enzymatic activity of monomeric NAA10-V111G but not for NAA10-V111G in complex with NAA15 (NatA enzymatic activity). A glycine in position 111 instead of valine will not cause any steric clashes, but loss of the more bulky hydrophobic side chain of valine may possibly cause structural alterations affecting protein stability or acetyl-CoA binding |
756297 |
| 2.3.1.255 | Y139A |
mutation in NatA, dramaitc loss of activity |
736866 |
| 2.3.1.255 | Y26A |
mutation in NatA, decrease in kcat, increase in Km value |
736866 |
| 2.3.1.255 | Y33A |
mutation in NatA, decrease in kcat, increase in Km value |
736866 |
| 2.3.1.255 | Y43S |
site-directed mutagenesis, the mutant is catalytically impaired in vitro, with approximately an 85% reduction in Nt-catalytic activity for peptide substrates EEEI, DDDI, and SESS |
756675 |
