Inhibition by glucosamine of myristoylation in human H9 lymphocytes and rat liver cells

FEBS Letters

Saermark, T.¹  Andreassen, H.¹  Jacobsen, C.¹ 

[1] Laboratory for Protein Chemistry, University of Copenhagen, Sigurdsgade 34, DK-2200 N Denmark

关键词: Fatty acid acylation;    Myristoylation;    Glucosamine;    N-Myristoyl transferase;   

DOI  :  10.1016/0014-5793(89)81502-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 p27nef a K _m value of 2.4 μM and a V _max of 240 per 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.

【 授权许可】

Unknown