Structural highlights
Function
NAT_SACS2 Displays alpha (N-terminal) acetyltransferase activity. Catalyzes the covalent attachment of an acetyl moiety from acetyl-CoA to the free alpha-amino group at the N-terminus of a protein (PubMed:17511810, PubMed:23959863, PubMed:25728374). NAT is able to acetylate the alpha-amino group of methionine, alanine and serine N-terminal residue substrates, however it has a preference for Ser-N-terminal substrates (PubMed:17511810, PubMed:23959863, PubMed:25728374).[1] [2] [3]
References
- ↑ Mackay DT, Botting CH, Taylor GL, White MF. An acetylase with relaxed specificity catalyses protein N-terminal acetylation in Sulfolobus solfataricus. Mol Microbiol. 2007 Jun;64(6):1540-8. doi: 10.1111/j.1365-2958.2007.05752.x. Epub , 2007 May 18. PMID:17511810 doi:http://dx.doi.org/10.1111/j.1365-2958.2007.05752.x
- ↑ Liszczak G, Marmorstein R. Implications for the evolution of eukaryotic amino-terminal acetyltransferase (NAT) enzymes from the structure of an archaeal ortholog. Proc Natl Acad Sci U S A. 2013 Sep 3;110(36):14652-7. doi:, 10.1073/pnas.1310365110. Epub 2013 Aug 19. PMID:23959863 doi:http://dx.doi.org/10.1073/pnas.1310365110
- ↑ Chang YY, Hsu CH. Structural Basis for Substrate-specific Acetylation of Nalpha-acetyltransferase Ard1 from Sulfolobus solfataricus. Sci Rep. 2015 Mar 2;5:8673. doi: 10.1038/srep08673. PMID:25728374 doi:http://dx.doi.org/10.1038/srep08673
