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#myristoylation

3 public questions tagged with this topic.

Lipid Link Protein

What type of bond formation occurs in myristoylation?

Myristoylation represents cotranslational irreversible lipidation catalyzed by cytosolic N-myristoyltransferases NMT1 and NMT2. After methionine aminopeptidase removes initiator methionine, glycine at position two becomes exposed as acceptor. NMT binds myristoyl-CoA, a fourteen-carbon saturated fatty acyl thioester, and transfers acyl chain to alpha-amino group of N-terminal glycine forming stable amide linkage resistant to neutral hydroxylamine, alkaline treatment, and reducing agents, unlike labile thioesters. The myristate provides approximately eight kilocalories per mol hydrophobic insert

Ref: Lodish et al., Molecular Cell Biology, 9th ed., Chapter 10, Protein Lipidation and Myristoylation.

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Lipid Link Protein

Which of the following lipid modifications involves thioether bond formation?

Lipid modifications differ in chemistry of linkage and reversibility. N-myristoylation forms amide bond between myristate and N-terminal glycine co-translationally irreversible, palmitoylation forms thioester between 16-carbon palmitate and cysteine thiol reversibly cleaved by acyl protein thioesterases, GPI anchoring forms amide between ethanolamine phosphate and C-terminus plus glycosidic linkages to inositol phospholipid. Prenylation, either farnesylation 15-carbon or geranylgeranylation 20-carbon, occurs at C-terminal CAAX motif where X determines farnesyl vs geranylgeranyl transferase spe

Ref: Wang & Casey, Nat Rev Mol Cell Biol 2016, Protein prenylation and thioether linkage.

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Lipid Link Protein

Which amino acid is commonly involved in myristoylation?

N-myristoylation is co-translational irreversible modification attaching 14-carbon saturated fatty acid myristate from myristoyl-CoA to target protein. N-myristoyltransferase NMT recognizes N-terminal sequence Met-Gly-X-X-X-Ser/Thr after methionine aminopeptidase removes initiator methionine, exposing glycine at position 2 for amide bond formation. The glycine requirement is absolute; replacement with other residues abolishes myristoylation. Myristate anchor provides weak membrane affinity that often cooperates with additional palmitoylation or polybasic cluster to stably tether proteins to in

Ref: Resh, Biochim Biophys Acta 1999, N-myristoylation mechanisms; Farah et al., J Biol Chem 2020, NMT specificity.

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