Issue 19, 2006

The design and synthesis of inhibitors of pantothenate synthetase

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

Supplementary files

Article information

Article type
Paper
Submitted
04 7 2006
Accepted
08 8 2006
First published
30 8 2006

Org. Biomol. Chem., 2006,4, 3598-3610

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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