Jump to main content
Jump to site search
Access to RSC content Close the message box

Continue to access RSC content when you are not at your institution. Follow our step-by-step guide.


Issue 6, 2011
Previous Article Next Article

Exploring Leishmania majorInositol Phosphorylceramide Synthase (LmjIPCS): Insights into the ceramide binding domain

Author affiliations

Abstract

The synthesis of set of ceramide analogues exploring hydrophobicity in the acyl chains and the degree and nature of hydroxylation is described. These have been assayed against the parasitic protozoan enzymeLmjIPCS. These studies showed that whilst the C-3 hydroxyl group was not essential for turnover it provided enhanced affinity. Reflecting the membrane bound nature of the enzyme a long (C13) hydrocarbon ceramide tail was necessary for both high affinity and turnover. Whilst the N-acyl chain also contributed to affinity, analogues lacking the amide linkage functioned as competitive inhibitors in both enzyme and cell-based assays. A model that accounts for this observation is proposed.

Graphical abstract: Exploring Leishmania majorInositol Phosphorylceramide Synthase (LmjIPCS): Insights into the ceramide binding domain

Back to tab navigation

Supplementary files

Article information


Submitted
12 Oct 2010
Accepted
13 Dec 2010
First published
26 Jan 2011

Org. Biomol. Chem., 2011,9, 1823-1830
Article type
Paper

Exploring Leishmania majorInositol Phosphorylceramide Synthase (LmjIPCS): Insights into the ceramide binding domain

J. G. Mina, J. A. Mosely, H. Z. Ali, P. W. Denny and P. G. Steel, Org. Biomol. Chem., 2011, 9, 1823
DOI: 10.1039/C0OB00871K

Social activity

Search articles by author

Spotlight

Advertisements