MyristoylCoA:protein N‐Myristoyltransferase: Probing Host‐Guest Interactions Using Synthetic Substrates

George W. Gokel, Tianbao Lu, David A. Rudnick, Emily Jackson‐Machelski, Jeffrey I. Gordon

Research output: Contribution to journalArticlepeer-review

3 Scopus citations

Abstract

MyristoylCoA:protein N‐myristoyl transferase (NMT) catalyzes the cotranslational covalent attachment of myristate (C14:0) to the ammo‐terminal glycine residues of a variety of biologically important proteins. An extensive survey of myristic acid analogs has previously allowed us to infer the conformational constraints imposed upon the fatty acid when bound to the enzyme's acylCoA binding site. A series of myristic acid analogs has now been synthesized and studied in an in vitro assay to probe further the conformation of NMT's bound ligand and to assess the importance of the distance between the carboxyl and the proposed bend in the fatty acid.

Original languageEnglish
Pages (from-to)127-133
Number of pages7
JournalIsrael Journal of Chemistry
Volume32
Issue number1
DOIs
StatePublished - 1992

Fingerprint

Dive into the research topics of 'MyristoylCoA:protein N‐Myristoyltransferase: Probing Host‐Guest Interactions Using Synthetic Substrates'. Together they form a unique fingerprint.

Cite this