peptide crotonyltransferase activity

Definition

Target type: molecularfunction

Catalysis of the reaction: crotonyl-CoA + lysine in peptide = CoA + N-crotonyl-lysine-peptide. [PMID:25818647]

Peptide crotonyltransferase activity refers to the enzymatic ability to catalyze the transfer of a crotonyl group from a donor molecule, such as crotonyl-CoA, to a specific amino acid residue within a peptide substrate. This enzymatic reaction involves the formation of a covalent bond between the crotonyl group and the amino acid side chain. Crotonylation is a post-translational modification that can alter the structure and function of proteins. It is a relatively newly discovered modification, and its specific biological roles are still being actively investigated. However, emerging evidence suggests that crotonylation plays a role in various cellular processes, including gene regulation, signal transduction, and protein stability. The enzyme responsible for this activity is known as crotonyltransferase. These enzymes are typically characterized by a conserved catalytic domain that facilitates the transfer reaction.'
"

Proteins (1)

Compounds (5)