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Issue 19, 2006
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The design and synthesis of inhibitors of pantothenate synthetase

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Abstract

Pantothenate synthetase catalyses the ATP-dependent condensation of D-pantoate and β-alanine to form pantothenate. Ten analogues of the reaction intermediate pantoyl adenylate, in which the phosphodiester is replaced by either an ester or sulfamoyl group, were designed as potential inhibitors of the enzyme. The esters were all modest competitive inhibitors, the sulfamoyls were more potent, consistent with their closer structural similarity to the pantoyl adenylate intermediate.

Graphical abstract: The design and synthesis of inhibitors of pantothenate synthetase

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Publication details

The article was received on 04 Jul 2006, accepted on 08 Aug 2006 and first published on 30 Aug 2006


Article type: Paper
DOI: 10.1039/B609482A
Citation: Org. Biomol. Chem., 2006,4, 3598-3610
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    The design and synthesis of inhibitors of pantothenate synthetase

    K. L. Tuck, S. A. Saldanha, L. M. Birch, A. G. Smith and C. Abell, Org. Biomol. Chem., 2006, 4, 3598
    DOI: 10.1039/B609482A

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