The Enzyme Database

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EC 2.3.1.256     
Accepted name: N-terminal methionine Nα-acetyltransferase NatC
Reaction: (1) acetyl-CoA + an N-terminal-L-methionyl-L-leucyl-[protein] = an N-terminal-Nα-acetyl-L-methionyl-L-leucyl-[protein] + CoA
(2) acetyl-CoA + an N-terminal-L-methionyl-L-isoleucyl-[protein] = an N-terminal-Nα-acetyl-L-methionyl-L-isoleucyl-[protein] + CoA
(3) acetyl-CoA + an N-terminal-L-methionyl-L-phenylalanyl-[protein] = an N-terminal-Nα-acetyl-L-methionyl-L-phenylalanyl-[protein] + CoA
(4) acetyl-CoA + an N-terminal-L-methionyl-L-tryptophyl-[protein] = an N-terminal-Nα-acetyl-L-methionyl-L-tryptophyl-[protein] + CoA
(5) acetyl-CoA + an N-terminal-L-methionyl-L-tyrosinyl-[protein] = an N-terminal-Nα-acetyl-L-methionyl-L-tyrosinyl-[protein] + CoA
Other name(s): NAA30 (gene name); NAA35 (gene name); NAA38 (gene name); MAK3 (gene name); MAK10 (gene name); MAK31 (gene name)
Systematic name: acetyl-CoA:N-terminal-Met-Leu/Ile/Phe/Trp/Tyr-[protein] Met Nα-acetyltransferase
Comments: N-terminal-acetylases (NATs) catalyse the covalent attachment of an acetyl moiety from acetyl-CoA to the free α-amino group at the N-terminus of a protein. This irreversible modification neutralizes the positive charge at the N-terminus and makes the N-terminal residue larger and more hydrophobic, and may also play a role in membrane targeting and gene silencing. The NatC complex is found in all eukaryotic organisms, and specifically targets N-terminal L-methionine residues attached to bulky hydrophobic residues at the second position, including Leu, Ile, Phe, Trp, and Tyr residues.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Polevoda, B. and Sherman, F. NatC Nα-terminal acetyltransferase of yeast contains three subunits, Mak3p, Mak10p, and Mak31p. J. Biol. Chem. 276 (2001) 20154–20159. [PMID: 11274203]
2.  Polevoda, B. and Sherman, F. Composition and function of the eukaryotic N-terminal acetyltransferase subunits. Biochem. Biophys. Res. Commun. 308 (2003) 1–11. [PMID: 12890471]
3.  Pesaresi, P., Gardner, N.A., Masiero, S., Dietzmann, A., Eichacker, L., Wickner, R., Salamini, F. and Leister, D. Cytoplasmic N-terminal protein acetylation is required for efficient photosynthesis in Arabidopsis. Plant Cell 15 (2003) 1817–1832. [PMID: 12897255]
4.  Wenzlau, J.M., Garl, P.J., Simpson, P., Stenmark, K.R., West, J., Artinger, K.B., Nemenoff, R.A. and Weiser-Evans, M.C. Embryonic growth-associated protein is one subunit of a novel N-terminal acetyltransferase complex essential for embryonic vascular development. Circ. Res. 98 (2006) 846–855. [PMID: 16484612]
5.  Starheim, K.K., Gromyko, D., Evjenth, R., Ryningen, A., Varhaug, J.E., Lillehaug, J.R. and Arnesen, T. Knockdown of human Nα-terminal acetyltransferase complex C leads to p53-dependent apoptosis and aberrant human Arl8b localization. Mol. Cell Biol. 29 (2009) 3569–3581. [PMID: 19398576]
[EC 2.3.1.256 created 1989 as EC 2.3.1.88, part transferred 2016 to EC 2.3.1.256]
 
 


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