Ontology highlight
ABSTRACT:
SUBMITTER: Rampoldi F
PROVIDER: S-EPMC3466015 | biostudies-literature | 2012 Nov
REPOSITORIES: biostudies-literature
Rampoldi Francesca F Sandhoff Roger R Owen Robert W RW Gröne Hermann-Josef HJ Porubsky Stefan S
Journal of lipid research 20120724 11
Myristoyl-CoA (CoA):protein N-myristoyltransferase (NMT) catalyzes protein modification through covalent attachment of a C14 fatty acid (myristic acid) to the N-terminal glycine of proteins, thus promoting protein-protein and protein-membrane interactions. NMT is essential for the viability of numerous human pathogens and is also up-regulated in several tumors. Here we describe a new, nonradioactive, ELISA-based method for measuring NMT activity. After the NMT-catalyzed reaction between a FLAG-t ...[more]