myristoyltransferase activity

Definition

Target type: molecularfunction

Catalysis of the transfer of a myristoyl (CH3-[CH2]12-CO-) group to an acceptor molecule. [GOC:ai]

Myristoyltransferase activity is the enzymatic process that attaches a myristate group, a 14-carbon saturated fatty acid, to a protein. This attachment, known as myristoylation, is a common post-translational modification that occurs at the N-terminal glycine residue of a protein. The myristate group is typically added through an amide linkage, forming a stable covalent bond. Myristoylation plays a crucial role in various cellular processes, including protein-protein interactions, membrane association, and signal transduction. It often targets proteins involved in cellular signaling, membrane trafficking, and cytoskeletal organization. Myristoylation can enhance protein-membrane interactions by anchoring the protein to the inner leaflet of the plasma membrane. This membrane association is crucial for the function of many proteins, including those involved in signal transduction, cell adhesion, and intracellular trafficking. Additionally, myristoylation can influence protein-protein interactions by modulating the conformation of the protein or by providing a specific binding site for other proteins. The process is typically catalyzed by enzymes called N-myristoyltransferases (NMTs). These enzymes are highly conserved across species and are responsible for transferring the myristate group from myristoyl-CoA to the N-terminal glycine residue of target proteins. The specificity of NMTs is determined by the sequence of the N-terminal region of the protein substrate. In addition to its role in protein function, myristoylation can also be involved in various cellular signaling pathways. For example, myristoylation of proteins involved in the Ras signaling pathway can regulate downstream signaling events and contribute to cell growth and proliferation.'
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Proteins (2)

Compounds (3)