Transferases;
Acyltransferases;
Transferring groups other than aminoacyl groups

acetyl-CoA:N-terminal-L-seryl-[histone 4/2A] L-serine Nalpha-acetyltransferase

(1) acetyl-CoA + an N-terminal-L-seryl-[histone H4] = an N-terminal-Nalpha-acetyl-L-seryl-[histone H4] + CoA;
(2) acetyl-CoA + an N-terminal-L-seryl-[histone H2A] = an N-terminal-Nalpha-acetyl-L-seryl-[histone H2A] + CoA

acetyl-CoA [CPD:C00024];
N-terminal-L-seryl-[histone H4];
N-terminal-L-seryl-[histone H2A]

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 and makes the N-terminal residue larger and more hydrophobic. NatD is found in all eukaryotic organisms, and acetylates solely the serine residue at the N-terminus of histones H2A or H4. Efficient recognition and acetylation by NatD requires at least the first 30 to 50 highly conserved amino acid residues of the histone N terminus.

EC 2.3.1.257 created 1989 as EC 2.3.1.88, part transferred 2016 to EC 2.3.1.257

1  [PMID:12915400]

Song OK, Wang X, Waterborg JH, Sternglanz R

An Nalpha-acetyltransferase responsible for acetylation of the N-terminal residues of histones H4 and H2A.

J Biol Chem 278:38109-12 (2003)
DOI:10.1074/jbc.C300355200

[sce:YMR069W]

2  [PMID:19332560]

Polevoda B, Hoskins J, Sherman F

Properties of Nat4, an N(alpha)-acetyltransferase of Saccharomyces cerevisiae that modifies N termini of histones H2A and H4.

Mol Cell Biol 29:2913-24 (2009)
DOI:10.1128/MCB.00147-08

3  [PMID:25619998]

Magin RS, Liszczak GP, Marmorstein R

The molecular basis for histone H4- and H2A-specific amino-terminal acetylation by NatD.

Structure 23:332-41 (2015)
DOI:10.1016/j.str.2014.10.025

[hsa:79829] [spo:SPCC825.04c]