We have developed a simple and rapid method for detecting the enzyme myristoyl-CoA:protein N-myristoyl transferase. The enzyme catalyzes the transfer of the myristoyl moiety of myristoyl-CoA to the amino-terminal glycine residue of a peptide (protein). Incorporation of the [14C]myristate into the pe
A Continuous Fluorometric Assay of Myristoyl-Coenzyme A:Protein N-Myristoyltransferase
โ Scribed by Cynthia R. Pennise; Nafsika H. Georgopapadakou; R.Dale Collins; Nilsa R. Graciani; David L. Pompliano
- Publisher
- Elsevier Science
- Year
- 2002
- Tongue
- English
- Weight
- 49 KB
- Volume
- 300
- Category
- Article
- ISSN
- 0003-2697
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โฆ Synopsis
Site-specific attachment of hydrophobic moieties to proteins (fatty acid acylation and prenylation) is a functionally essential modification involved in intracellular signaling pathways (1-3). Study of the transferase enzymes that catalyze these modifications is complicated by troublesome single point methods for assaying their activity. We have developed a continuous fluorometric assay for one of these enzymes, myristoyl-CoA 2 :protein N-myristoyltransferase (Nmt), useful for high-throughput assays and enzyme kinetics studies.
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