ID   2.3.1.258
DE   N-terminal methionine N(alpha)-acetyltransferase NatE.
CA   (1) acetyl-CoA + N-terminal L-methionyl-L-alanyl-[protein] = CoA + H(+) +
CA   N-terminal N(alpha)-acetyl-L-methionyl-L-alanyl-[protein].
CA   (2) acetyl-CoA + N-terminal L-methionyl-L-seryl-[protein] = CoA + H(+) +
CA   N-terminal N(alpha)-acetyl-L-methionyl-L-seryl-[protein].
CA   (3) acetyl-CoA + N-terminal L-methionyl-L-valyl-[protein] = CoA + H(+) +
CA   N-terminal N(alpha)-acetyl-L-methionyl-L-valyl-[protein].
CA   (4) acetyl-CoA + N-terminal L-methionyl-L-threonyl-[protein] = CoA + H(+)
CA   + N-terminal N(alpha)-acetyl-L-methionyl-L-threonyl-[protein].
CA   (5) acetyl-CoA + N-terminal L-methionyl-L-lysyl-[protein] = CoA + H(+) +
CA   N-terminal N(alpha)-acetyl-L-methionyl-L-lysyl-[protein].
CA   (6) acetyl-CoA + N-terminal L-methionyl-L-leucyl-[protein] = CoA + H(+) +
CA   N-terminal N(alpha)-acetyl-L-methionyl-L-leucyl-[protein].
CA   (7) acetyl-CoA + N-terminal L-methionyl-L-phenylalanyl-[protein] = CoA +
CA   H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-phenylalanyl-[protein].
CA   (8) acetyl-CoA + N-terminal L-methionyl-L-tyrosyl-[protein] = CoA + H(+)
CA   + N-terminal N(alpha)-acetyl-L-methionyl-L-tyrosyl-[protein].
CC   -!- N-terminal-acetylases (NATs) catalyze the covalent attachment of an
CC       acetyl moiety from acetyl-CoA to the free alpha-amino group at the
CC       N-terminus of a protein.
CC   -!- This irreversible modification neutralizes the positive charge at the
CC       N-terminus, makes the N-terminal residue larger and more hydrophobic,
CC       and prevents its removal by hydrolysis.
CC   -!- It may also play a role in membrane targeting and gene silencing.
CC   -!- NatE is found in all eukaryotic organisms and plays an important role
CC       in chromosome resolution and segregation.
CC   -!- It specifically targets N-terminal L-methionine residues attached to
CC       Lys, Val, Ala, Tyr, Phe, Leu, Ser, and Thr.
CC   -!- There is some substrate overlap with EC 2.3.1.256.
CC   -!- In addition, the acetylation of Met followed by small residues such
CC       as Ser, Thr, Ala, or Val suggests a kinetic competition between
CC       NatE and EC 3.4.11.18.
CC   -!- The enzyme also has the activity of EC 2.3.1.48 and autoacetylates
CC       several of its own lysine residues.
CC   -!- Formerly EC 2.3.1.88.
DR   Q0IIJ0, NAA50_BOVIN;  Q6DBY2, NAA50_DANRE;  Q9GZZ1, NAA50_HUMAN;
DR   Q6PGB6, NAA50_MOUSE;  Q5RF28, NAA50_PONAB;  Q6GP53, NAA50_XENLA;
DR   Q5XGA9, NAA50_XENTR;  Q08689, NAT5_YEAST ;  Q980R9, NAT_SACS2  ;
DR   Q4JBG0, NAT_SULAC  ;  Q976C3, NAT_SULTO  ;  I6YG32, RIMI_MYCTU ;
DR   Q9NHD5, SAN_DROME  ;
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