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Protein N-myristoylation

Authors :
George W. Gokel
S P Adams
Robert J. Duronio
David A. Rudnick
Jeffrey I. Gordon
Source :
Journal of Biological Chemistry. 266:8647-8650
Publication Year :
1991
Publisher :
Elsevier BV, 1991.

Abstract

Protein N-myristoylation refers to the covalent attachment of myristic acid, a 14-carbon saturated fatty acid (C14:0), to the N-terminal glycine of proteins. Linkage occurs via an amide bond and takes place as proteins are being synthesized. N-myristoylproteins have varied intracellular destinations, and are involved in myriad cellular functions ranging from signal transduction to protein and vesicular trafficking. N-myristoylproteins are encountered in members of all kingdoms of the eukaryotic domain (Protist, Fungi, Plant, and Animal), but are not produced by members of Bacteria or Archaea. MyristoylCoA: protein N-myristoyltransferase (Nmt), E.C. 2.3.1.97, a member of the GCN5 acetyltransferase (GNAT) superfamily, is responsible for catalyzing the transfer of myristate from myristoylCoA to proteins. While the acylCoA substrate specificity of Nmt has been highly conserved during evolution, its peptide substrate specificities have diverged among eukaryotes.

Details

ISSN :
00219258
Volume :
266
Database :
OpenAIRE
Journal :
Journal of Biological Chemistry
Accession number :
edsair.doi...........afa9c32fdb7a6eec89cf8465dc2c60da
Full Text :
https://doi.org/10.1016/s0021-9258(18)31490-x