peptide alpha-N-acetyltransferase activity

Definition

Target type: molecularfunction

Catalysis of the reaction: acetyl-CoA + peptide = CoA + N-alpha-acetylpeptide. This reaction is the acetylation of the N-terminal amino acid residue of a peptide or protein. [GOC:mah, PMID:30054468]

Peptide alpha-N-acetyltransferase activity is a molecular function that involves the enzymatic transfer of an acetyl group from acetyl-CoA to the N-terminal amino group of a peptide. This process is critical for various cellular functions, including protein stability, protein folding, protein degradation, and protein-protein interactions. The acetyl group, a small molecule consisting of a methyl group linked to a carbonyl group, is transferred from the coenzyme acetyl-CoA to the N-terminus of the peptide. This transfer reaction is catalyzed by a specific enzyme called peptide alpha-N-acetyltransferase. The addition of the acetyl group to the N-terminus of a peptide can alter its chemical properties, including its charge, hydrophobicity, and conformation. This can influence the peptide's stability, its ability to interact with other molecules, and its susceptibility to degradation. For example, acetylation can increase the stability of proteins by preventing their degradation by proteases. Furthermore, acetylation can influence protein folding by promoting the formation of specific secondary structures. In addition, acetylation can alter the ability of proteins to interact with other molecules, such as DNA, RNA, or other proteins. In summary, peptide alpha-N-acetyltransferase activity is an essential molecular function that plays a critical role in the regulation of protein structure, stability, and function.'
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Proteins (1)

Compounds (2)