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@article{Goncalves:2012:10.1016/j.ab.2011.10.013,
author = {Goncalves, V and Brannigan, JA and Thinon, E and Olaleye, TO and Serwa, R and Lanzarone, S and Wilkinson, AJ and Tate, EW and Leatherbarrow, RJ},
doi = {10.1016/j.ab.2011.10.013},
journal = {Analytical Biochemistry},
pages = {342--344},
title = {A fluorescence-based assay for N-myristoyltransferase activity},
url = {http://dx.doi.org/10.1016/j.ab.2011.10.013},
volume = {421},
year = {2012}
}
TY - JOUR
AB - N-myristoylation is the irreversible attachment of a C14 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.
AU - Goncalves,V
AU - Brannigan,JA
AU - Thinon,E
AU - Olaleye,TO
AU - Serwa,R
AU - Lanzarone,S
AU - Wilkinson,AJ
AU - Tate,EW
AU - Leatherbarrow,RJ
DO - 10.1016/j.ab.2011.10.013
EP - 344
PY - 2012///
SN - 1096-0309
SP - 342
TI - A fluorescence-based assay for N-myristoyltransferase activity
T2 - Analytical Biochemistry
UR - http://dx.doi.org/10.1016/j.ab.2011.10.013
UR - http://hdl.handle.net/10044/1/26864
VL - 421
ER -
Prof. Ed Tate
GSK Chair in Chemical Biology
Department of Chemistry
Molecular Sciences Research Hub, White City Campus,
82 Wood Lane, London, W12 0BZ
e.tate@imperial.ac.uk
Tel: +44 (0)20 759 + ext 43752 or 45821