| A fluorescence-based assay for N-myristoyltransferase activity. | |
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MedLine Citation:
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PMID: 22051857 Owner: NLM Status: Publisher |
Abstract/OtherAbstract:
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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. |
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Authors:
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Victor Goncalves; James A Brannigan; Emmanuelle Thinon; Tayo O Olaleye; Remigiusz Serwa; Salvatore Lanzarone; Anthony J Wilkinson; Edward W Tate; Robin J Leatherbarrow |
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Publication Detail:
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Type: JOURNAL ARTICLE Date: 2011-10-14 |
Journal Detail:
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Title: Analytical biochemistry Volume: - ISSN: 1096-0309 ISO Abbreviation: - Publication Date: 2011 Oct |
Date Detail:
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Created Date: 2011-11-4 Completed Date: - Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 0370535 Medline TA: Anal Biochem Country: - |
Other Details:
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Languages: ENG Pagination: - Citation Subset: - |
Copyright Information:
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Copyright © 2011 Elsevier Inc. All rights reserved. |
Affiliation:
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Department of Chemistry, Imperial College London, London SW7 2AZ, UK. |
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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