Literature DB >> 22051857

A fluorescence-based assay for N-myristoyltransferase activity.

Victor Goncalves1, James A Brannigan, Emmanuelle Thinon, Tayo O Olaleye, Remigiusz Serwa, Salvatore Lanzarone, Anthony J Wilkinson, Edward W Tate, Robin J Leatherbarrow.   

Abstract

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.
Copyright © 2011 Elsevier Inc. All rights reserved.

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Year:  2011        PMID： 22051857      PMCID： PMC3863716          DOI： 10.1016/j.ab.2011.10.013

Source DB:  PubMed          Journal:  Anal Biochem        ISSN： 0003-2697            Impact factor:   3.365


  22 in total

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