Imperial College London
Professor Robin Leatherbarrow

ProfessorRobinLeatherbarrow

Faculty of Natural Sciences, Department of Chemistry

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Contact

 

r.leatherbarrow Website

 
 
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Location

 

ChemistrySouth Kensington Campus

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Summary

 

Publications

Citation

BibTex format

@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}
}
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RIS format (EndNote, RefMan)

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  -
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