protein-cysteine S-myristoyltransferase activity

Definition

Target type: molecularfunction

Catalysis of the transfer of a myristoyl (systematic name, tetradecanoyl) group to a sulfur atom on a cysteine residue of a protein molecule in the reaction: tetradecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-tetradecanoyl-L-cysteinyl-[protein]. [GOC:ai, PMID:22247542, RHEA:59736]

Protein-cysteine S-myristoyltransferase activity is a crucial enzymatic function that plays a vital role in cellular signaling and protein targeting. This activity involves the covalent attachment of myristate, a 14-carbon saturated fatty acid, to the N-terminal glycine residue of specific proteins. This process, known as myristoylation, is an irreversible modification that serves as a molecular switch, influencing protein localization, interactions, and ultimately, their biological functions.

Myristoylation typically occurs during or immediately after protein synthesis. It is catalyzed by a family of enzymes called N-myristoyltransferases (NMTs). NMTs recognize specific sequence motifs within the target protein, typically an N-terminal glycine residue followed by a few hydrophobic amino acids. Once the myristate is attached, it becomes a critical component of the protein's structure, often serving as a hydrophobic anchor that facilitates membrane association.

Myristoylation has a profound impact on protein function. It can:

- **Promote membrane association:** The hydrophobic myristate group can insert into the lipid bilayer of cellular membranes, anchoring the protein to the membrane surface. This is essential for proteins involved in signal transduction, membrane trafficking, and other membrane-associated processes.
- **Facilitate protein-protein interactions:** The myristate group can act as a binding site for other proteins, influencing their interactions and assembly into larger complexes.
- **Regulate protein activity:** Myristoylation can alter the conformation or stability of a protein, thereby modulating its enzymatic activity or its ability to interact with other molecules.

Myristoylation is a highly conserved process found across diverse organisms, highlighting its fundamental importance in cellular function. Aberrant myristoylation has been implicated in various diseases, including cancer and viral infections. Therefore, understanding the molecular mechanisms of myristoylation is crucial for developing new therapeutic strategies targeting these conditions.'
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Proteins (1)

Compounds (1)