N-terminal protein N-methyltransferase activity

Definition

Target type: molecularfunction

Catalysis of the transfer of a methyl group from S-adenosyl-L-methionine (AdoMet) to the alpha-amino group of the N-terminal amino or imino acid residue of a protein substrate. For example, yeast Tae1p and mammalian family member METTL11A preferentially modify the N-terminal residue of substrates with the N-terminal sequence X-Pro-Lys, where X can be Pro, Ala, or Ser. [PMID:20481588]

N-terminal protein N-methyltransferase activity refers to the enzymatic process of transferring a methyl group from a methyl donor, such as S-adenosyl methionine (SAM), to the N-terminal amino group of a protein. This modification, known as N-terminal methylation, plays a crucial role in various cellular processes, including protein folding, stability, and interaction with other molecules. N-terminal methylation can also influence the activity and localization of proteins.

The catalytic mechanism typically involves the formation of a ternary complex between the enzyme, the protein substrate, and SAM. The enzyme utilizes a conserved catalytic domain to bind SAM and facilitate the transfer of the methyl group to the N-terminal amino group of the protein substrate. The specificity of N-terminal protein N-methyltransferases is often determined by the sequence of the N-terminal region of the protein substrate, and some enzymes display a preference for specific amino acids at the N-terminus.

N-terminal protein N-methyltransferases are found in various organisms, from bacteria to humans, and are involved in diverse biological functions. For example, in bacteria, N-terminal methylation can contribute to resistance to antibiotics. In eukaryotes, N-terminal methylation plays a role in regulating protein stability, protein-protein interactions, and cellular signaling pathways.

Overall, N-terminal protein N-methyltransferase activity is an important post-translational modification that contributes significantly to the regulation of protein function and cellular processes.'
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Proteins (1)

Compounds (1)