Acetylation

Acetylation is the addition of an acetyl group, CH₃CO–, to a molecule. It can alter a molecule’s chemical properties, activity, or interactions.

Acetyl group: A chemical group consisting of a carbonyl bonded to a methyl group, written CH₃CO–. This is the group added in every acetylation reaction.
Histone acetylation: The addition of acetyl groups to lysine residues in histone proteins. This well-studied form of acetylation helps regulate access to DNA.
Acetylation reaction: A chemical reaction that transfers an acetyl group to an atom or molecule. It describes the underlying chemical event across biological and synthetic contexts.
Methylation: The addition of a methyl group to a molecule. It changes molecular properties through a smaller group than acetylation.
Acetyl-CoA: A coenzyme that carries an acetyl group in metabolism and many acetyl-transfer reactions. Cells commonly use it as the donor of acetyl groups.
Lysine acetylation: The attachment of an acetyl group to the amino group of a lysine residue. It modifies histones and many non-histone proteins.
Amide bond: A covalent bond between a carbonyl carbon and a nitrogen atom. N-acetylation commonly creates an amide linkage.
Phosphorylation: The addition of a phosphate group to a molecule, often catalyzed by a kinase. It is another reversible protein modification, with different chemical effects.
Acetyltransferase: An enzyme that transfers an acetyl group from a donor molecule to an acceptor. These enzymes catalyze many selective acetylation reactions.
N-terminal acetylation: The addition of an acetyl group to the amino terminus of a protein. This common protein modification can affect stability and interactions.

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