Inhibition of Mycobacterium tuberculosis pantothenate synthetase by analogues of the reaction intermediate.

Alessio Ciulli; D.E. Scott; M. Ando; Fernando Reyes; S. Adrian Saldanha; K.L. Tuck; D.Y. Chirgadze; T.L. Blundell; C. Abell

doi:10.1002/cbic.200800437

Inhibition of Mycobacterium tuberculosis pantothenate synthetase by analogues of the reaction intermediate.

Alessio Ciulli (Lead / Corresponding author), D.E. Scott, M. Ando, Fernando Reyes, S. Adrian Saldanha, K.L. Tuck, D.Y. Chirgadze, T.L. Blundell, C. Abell (Lead / Corresponding author)

Research output: Contribution to journal › Article › peer-review

60 Citations (Scopus)

Abstract

Get stuck in: Pantothenate synthetase is an attractive target for the development of novel small-molecule drugs against Mycobacterium tuberculosis. Three related sulfamoyl adenylate inhibitors were designed to closely mimic the structure of the reaction intermediate, pantoyl adenylate. The most potent inhibitor exhibited dissociation and inhibition constants of about 100 nM. The structural elucidation of the compounds bound to the enzyme will aid development of subsequent inhibitors.

Original language	English
Pages (from-to)	2606-2611
Number of pages	6
Journal	ChemBioChem
Volume	9
Issue number	16
DOIs	https://doi.org/10.1002/cbic.200800437
Publication status	Published - 3 Nov 2008

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abstract = "Get stuck in: Pantothenate synthetase is an attractive target for the development of novel small-molecule drugs against Mycobacterium tuberculosis. Three related sulfamoyl adenylate inhibitors were designed to closely mimic the structure of the reaction intermediate, pantoyl adenylate. The most potent inhibitor exhibited dissociation and inhibition constants of about 100 nM. The structural elucidation of the compounds bound to the enzyme will aid development of subsequent inhibitors.",

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AU - Ando, M.

AU - Reyes, Fernando

AU - Saldanha, S. Adrian

AU - Tuck, K.L.

AU - Chirgadze, D.Y.

AU - Blundell, T.L.

AU - Abell, C.

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AB - Get stuck in: Pantothenate synthetase is an attractive target for the development of novel small-molecule drugs against Mycobacterium tuberculosis. Three related sulfamoyl adenylate inhibitors were designed to closely mimic the structure of the reaction intermediate, pantoyl adenylate. The most potent inhibitor exhibited dissociation and inhibition constants of about 100 nM. The structural elucidation of the compounds bound to the enzyme will aid development of subsequent inhibitors.

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Inhibition of Mycobacterium tuberculosis pantothenate synthetase by analogues of the reaction intermediate.

Abstract

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