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Exploring Leishmania major inositol phosphorylceramide synthase (LmjIPCS) : insights into the ceramide binding domain.

Mina, J.G. and Mosely, J.A. and Ali, H.Z. and Denny, P.W. and Steel, P.G. (2011) 'Exploring Leishmania major inositol phosphorylceramide synthase (LmjIPCS) : insights into the ceramide binding domain.', Organic & biomolecular chemistry., 9 (6). pp. 1823-1830.

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 enzyme LmjIPCS. 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.

Item Type:Article
Full text:PDF - Accepted Version (808Kb)
Status:Peer-reviewed
Publisher Web site:http://dx.doi.org/10.1039/c0ob00871
Record Created:08 Mar 2011 10:20
Last Modified:13 Jan 2012 12:56

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