2.3.1.258 F27A site-directed mutagenesis, inactive mutant 719976 2.3.1.258 F27A the mutant shows less than 10% of wild type catalytic efficiency 719976 2.3.1.258 F35A site-directed mutagenesis, inactive mutant 719976 2.3.1.258 F35A the mutant shows less than 10% of wild type catalytic efficiency 719976 2.3.1.258 H112A inactive 720002 2.3.1.258 H112A NMR spectroscopy using the catalytically inactive hNaa50p mutant 720002 2.3.1.258 H112A site-directed mutagenesis, inactive mutant 719976 2.3.1.258 H112A the mutant shows less than 10% of wild type catalytic efficiency 719976 2.3.1.258 H112F site-directed mutagenesis, inactive mutant 719976 2.3.1.258 H112F the mutant shows less than 10% of wild type catalytic efficiency 719976 2.3.1.258 I142A site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme 719976 2.3.1.258 I142A the mutant shows 42.2% of wild type catalytic efficiency 719976 2.3.1.258 L814P site-directed mutagenesis, the hNAA15 mutant is defective for HYPK inhibition and reduces hNatA thermostability, hNAA10 binding is not affected 757754 2.3.1.258 additional information generation of mutants MtRimI4-158, MtRimI1-153, MtRimI4-153, MtRimIC21A, and of the final construct MtRimIC21A4-153, MtRimIC21A4-153 has almost identical enzymatic activity compared to MtRimI, indicating insignificant influence of the recombinant variations on enzymatic functions. The 2D 1H-15N heteronuclear single quantum coherence spectrum of tRimIC21A4-153 exhibits wider chemical shift dispersion and favorable peak isolation, indicating that MtRimIC21A4-153 is amendable for further structural determination. Moreover, bio-layer interferometry experiments show that MtRimIC21A4-153 possesses similar micromolar affinity to full-length MtRimI for binding the hexapeptide substrate Ala-Arg-Tyr-Phe-Arg-Arg. Structure comparison of wild-type MtRimI and mutant MtRimIC21A4-153 -, 755712 2.3.1.258 additional information N-terminal analyses comparing wild-type and scNaa50 deletion strains of Saccharomyces cerevisiae -, 758492 2.3.1.258 additional information recombinant GST-tagged hNaa50 fails to pull down Schizosaccharomyces pombe SpNatA and hNaa50 and SpNatA cannot form a stoichiometric complex -, 758493 2.3.1.258 P28A site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme 719976 2.3.1.258 P28A the mutant shows less 13.4% of wild type catalytic efficiency 719976 2.3.1.258 T406Y site-directed mutagenesis, the hNAA15 mutant can disassociate hNAA50 from hNatA in vitro, hNAA10 binding is not affected 757754 2.3.1.258 V29A site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme 719976 2.3.1.258 V29A the mutant shows 12.3% of wild type catalytic efficiency 719976 2.3.1.258 Y124F the mutant shows decreased activity compared to the wild type enzyme 740792 2.3.1.258 Y139A site-directed mutagenesis, inactive mutant 719976 2.3.1.258 Y139A the mutant shows less than 10% of wild type catalytic efficiency 719976 2.3.1.258 Y31A site-directed mutagenesis, inactive mutant 719976 2.3.1.258 Y31A the mutant shows less than 10% of wild type catalytic efficiency 719976 2.3.1.258 Y73A site-directed mutagenesis, inactive mutant 719976 2.3.1.258 Y73A the mutant shows less than 10% of wild type catalytic efficiency 719976 2.3.1.258 Y73F site-directed mutagenesis, inactive mutant 719976 2.3.1.258 Y73F the mutant shows less than 10% of wild type catalytic efficiency 719976