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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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Supplementary files

Article information


Submitted
04 Jul 2006
Accepted
08 Aug 2006
First published
30 Aug 2006

Org. Biomol. Chem., 2006,4, 3598-3610
Article type
Paper

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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