Target type: biologicalprocess
The myristoylation of the N-terminal glycine of proteins to form the derivative N-myristoyl-glycine. [RESID:AA0059]
N-terminal peptidyl-glycine N-myristoylation is a crucial post-translational modification that attaches myristate, a 14-carbon saturated fatty acid, to the N-terminal glycine residue of a protein. This process plays a vital role in protein-lipid interactions, membrane association, and signal transduction. The modification is catalyzed by N-myristoyltransferase (NMT), an enzyme that specifically recognizes the N-terminal glycine residue followed by a specific amino acid sequence. This sequence often includes a proline or methionine residue at the second position and is termed the myristoylation signal. The myristoylation process begins with the activation of myristate by the NMT enzyme, which involves the formation of a myristoyl-CoA intermediate. This activated myristate is then transferred to the N-terminal glycine residue of the target protein, forming an amide linkage. The transfer reaction requires the presence of a divalent cation, typically magnesium, as a cofactor. N-myristoylation can occur cotranslationally or posttranslationally. Cotranslational myristoylation happens as the protein is being synthesized on the ribosome, while posttranslational myristoylation occurs after the protein has been fully translated. N-myristoylation plays a critical role in various cellular processes, including: 1. Membrane targeting: Myristoylation allows proteins to associate with membranes, enabling them to perform specific functions within the cell. 2. Protein-protein interactions: The hydrophobic myristate moiety can facilitate protein-protein interactions by mediating the association of proteins to other membrane-bound components. 3. Signal transduction: Myristoylated proteins can act as signaling molecules, participating in pathways that control cell growth, differentiation, and other essential cellular processes. N-myristoylation is a highly conserved process across different species, highlighting its importance in biological systems. Dysregulation of N-myristoylation has been implicated in various human diseases, including cancer and neurodegenerative disorders. This makes N-myristoylation an attractive target for therapeutic intervention.'
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Protein | Definition | Taxonomy |
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Glycylpeptide N-tetradecanoyltransferase 1 | A glycylpeptide N-tetradecanoyltransferase 1 that is encoded in the genome of human. [PRO:WCB, UniProtKB:P30419] | Homo sapiens (human) |
Glycylpeptide N-tetradecanoyltransferase 2 | A glycylpeptide N-tetradecanoyltransferase 2 that is encoded in the genome of human. [PRO:DNx, UniProtKB:O60551] | Homo sapiens (human) |
Compound | Definition | Classes | Roles |
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sc 58272 | SC 58272: inhibits myristoyl-CoA:protein N-myristoyltransferase; structure given in first source | ||
maleic acid anilide | maleic acid anilide: structure given in first source | ||
ddd 85646 | DDD 85646: a trypanocidal agent for treating African sleeping sickness; structure in first source |