A fluorescence-based assay for N-myristoyltransferase activity

Victor Goncalves, James A. Brannigan, Emmanuelle Thinon, Tayo O. Olaleye, Remigiusz Serwa, Salvatore Lanzarone, Anthony J. Wilkinson, Edward W. Tate, Robin J. Leatherbarrow

Research output: Contribution to journalArticlepeer-review


N-myristoylation is the irreversible attachment of a C-14 fatty acid, myristic acid, to the N-terminal glycine of a protein via formation of an amide bond. This modification is catalyzed by myristoyl-coenzyme A (CoA):protein N-myristoyltransferase (NMT), an enzyme ubiquitous in eukaryotes that is up-regulated in several cancers. Here we report a sensitive fluorescence-based assay to study the enzymatic activity of human NMT1 and NMT2 based on detection of CoA by 7-diethylamino-3-(4-maleimido-phenyl)-4-methylcoumarin. We also describe expression and characterization of NMT1 and NMT2 and assay validation with small molecule inhibitors. This assay should be broadly applicable to NMTs from a range of organisms. (C) 2011 Elsevier Inc. All rights reserved.

Original languageEnglish
Pages (from-to)342-344
Number of pages3
Issue number1
Publication statusPublished - 1 Feb 2012

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