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Inhibition by glucosamine of myristoylation in human H9 lymphocytes and rat liver cells
Author(s) -
Jacobsen C.,
Andreassen H.,
Saermark T.
Publication year - 1989
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(89)81502-9
Subject(s) - glucosamine , myristoylation , myristic acid , in vitro , chemistry , biochemistry , peptide , in vivo , acylation , microbiology and biotechnology , biology , membrane , palmitic acid , fatty acid , catalysis
N ‐Myristoyl transferase (NMT) activity was measured in rat liver and H9 cells using an in vitro assay based on acylation of synthetic peptides. Glucosamine was found to inhibit the NMT activity. Using a synthetic peptide mimicking the N‐terminus of HIV p27 nef a K m value of 2.4 μM and a V max of 240per h was found. In the presence of glucosamine the V max was lowered indicating that glucosamine acted as a non‐competitive inhibitor. Glucosamine also inhibited incorporation of radiolabelled myristic acid into H9 cell proteins in vivo. In liver cells using a peptide from the N‐terminus of p60 SRC only the V max was affected.