PMID:16990935
| Citation |
Tuck, KL, Saldanha, SA, Birch, LM, Smith, AG and Abell, C (2006) The design and synthesis of inhibitors of pantothenate synthetase. Org. Biomol. Chem. 4:3598-610 |
|---|---|
| Abstract |
Pantothenate synthetase catalyses the ATP-dependent condensation of D-pantoate and beta-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. |
| Links |
PubMed Online version:10.1039/b609482a |
| Keywords |
Adenosine Triphosphate/pharmacology; Enzyme Inhibitors/chemical synthesis; Enzyme Inhibitors/chemistry; Enzyme Inhibitors/pharmacology; Escherichia coli/drug effects; Escherichia coli/enzymology; Esters/chemistry; Kinetics; Models, Molecular; Peptide Synthases/antagonists & inhibitors; Peptide Synthases/chemistry; Protein Structure, Secondary; Sulfonamides/chemistry; Temperature |
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