I think what you mean is myristilation of proteins. Usually, this kind
of protein modification is the attachment of single myristic acid to the
N-terminal glycine through an amide linkage, the linkage is the same as
peptide bond. In most myristilated proteins, the modification occurs at
a conserved motif. I think there is not any enzyme that can cut this
bond. It is different from the modification with C16 or C18 fatty acids,
which is cleavable with enzymes, and can be removed by reducing agents.
Besides, myristilated proteins are soluble in detergents, and are not
necessary associated with membrane all the time, like ras proteins.
Univ. of california, Davis