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2.3.1.258: N-terminal methionine Nalpha-acetyltransferase NatE

This is an abbreviated version!
For detailed information about N-terminal methionine Nalpha-acetyltransferase NatE, go to the full flat file.

Word Map on EC 2.3.1.258

Reaction

acetyl-CoA
+
an N-terminal-L-methionyl-L-alanyl-[protein]
=
an N-terminal-Nalpha-acetyl-L-methionyl-L-alanyl-[protein]
+
CoA

Synonyms

ARD1, EC 2.3.1.88, hNaa50, hNatA, MtRimI, N-terminal acetyltransferase E, NAA10, NAA15, Naa50, Naa50/San, Naa50p, Naa50p (NAT5/SAN) N-terminal acetyltransferase complex, Nalpha-acetyltransferase, NAT, NAT1, NAT5, NAT5/SAN, NatA, NatA/Naa50 complex, NatE, RimI, RimI acetyltransferase, Rv3420c, SAN, ScNaa50, ScNatA, SpNaa50, SpNatA

ECTree

     2 Transferases
         2.3 Acyltransferases
             2.3.1 Transferring groups other than aminoacyl groups
                2.3.1.258 N-terminal methionine Nalpha-acetyltransferase NatE

Systematic Name

Systematic Name on EC 2.3.1.258 - N-terminal methionine Nalpha-acetyltransferase NatE

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SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:N-terminal-Met-Ala/Ser/Val/Thr/Lys/Leu/Phe/Tyr-[protein] Met-Nalpha-acetyltransferase
N-terminal-acetylases (NATs) catalyse the covalent attachment of an acetyl moiety from acetyl-CoA to the free alpha-amino group at the N-terminus of a protein. This irreversible modification neutralizes the positive charge at the N-terminus, makes the N-terminal residue larger and more hydrophobic, and prevents its removal by hydrolysis. It may also play a role in membrane targeting and gene silencing. NatE is found in all eukaryotic organisms and plays an important role in chromosome resolution and segregation. It specifically targets N-terminal L-methionine residues attached to Lys, Val, Ala, Tyr, Phe, Leu, Ser, and Thr. There is some substrate overlap with EC 2.3.1.256, N-terminal methionine Nalpha-acetyltransferase NatC. In addition, the acetylation of Met followed by small residues such as Ser, Thr, Ala, or Val suggests a kinetic competition between NatE and EC 3.4.11.18, methionyl aminopeptidase. The enzyme also has the activity of EC 2.3.1.48, histone acetyltransferase, and autoacetylates several of its own lysine residues.