Myristic acid analogs that are putative inhibitors of N‐myristoyl‐transferase were tested in
vitro for activity against yeasts (Saccharomyces cerevisiae, Candida albicans, Cryptococcus …

N-Myristoyltransferase (NMT) is an emerging therapeutic target that catalyzes the
attachment of myristate to the N terminus of an acceptor protein. We have developed a …

Research has indicated that N-myristoyl transferase, an enzyme that catalyzes the addition
of a myristate group to the N-terminal glycine residues of proteins, is involved in the …

Several substrate and product analogs were synthesized and tested as in vitro inhibitors of
bovine brain N-myristoyl-CoA: protein N-myristoyltransferase (NMT; EC 2.3. 1.97). At 40 μM …

1. Two non-hydrolysable analogues of myristoyl-coenzyme A were synthesised and
spectroscopically characterized. Myristoyl-carba (dethk) coenzyme A was prepared in a …

We have explored the acyl-CoA substrate specificity of Saccharomyces cerevisiae myristoyl-
CoA: protein N-myristoyltransferase (NMT) by synthesizing 81 fatty acid analogs and …

Covalent attachment of myristic acid (C14: 0) to the amino-terminal glycine residue of a
variety of eukaryotic cellular and viral proteins can have a profound influence on their …

Protein N-myristoylation is a covalent modification that occurs co-translationally in
eukaryotes. Myristate, a rare 14 carbon saturated fatty acid (C14: 0), is attached, via an …

Myristoyl CoA: protein N-myristoyltransferase (NMT) catalyzes the addition of myristic acid to
the amino-terminal glycine residues of a number of eukaryotic proteins. Recently, we …

A variety of eukaryotic viral and cellular proteins possesses an NH2-terminal N-
myristoylglycine residue important for their biological functions. Recent studies of the …