Arabinose 5-phosphate isomerase as a target for antibacterial design : studies with substrate analogues and inhibitors
Articolo
Data di Pubblicazione:
2014
Citazione:
Arabinose 5-phosphate isomerase as a target for antibacterial design : studies with substrate analogues and inhibitors / L. Gabrielli, S. Merlo, C. Airoldi, P. Sperandeo, S. Gianera, A. Polissi, F. Nicotra, T.P. Holler, R.W. Woodard, L. Cipolla. - In: BIOORGANIC & MEDICINAL CHEMISTRY. - ISSN 0968-0896. - 22:8(2014), pp. 2576-2583. [10.1016/j.bmc.2013.08.012]
Abstract:
Structural requirements of d-arabinose 5-phosphate isomerase (KdsD, E.C. 5.3.1.13) from Pseudomonas aeruginosa were analysed in detail using advanced NMR techniques. We performed epitope mapping studies of the binding between the enzyme and the most potent KdsD inhibitors found to date, together with studies of a set of newly synthesised arabinose 5-phosphate (A5P) mimetics. We report here the first experimental evidence that KdsD may bind the furanose form of A5P, suggesting that catalysis of ring opening may be an important part of KdsD catalysis.
Tipologia IRIS:
01 - Articolo su periodico
Keywords:
d-Arabinose 5-phosphate isomerase; Enzyme inhibitors; Escherichia coli; Molecular recognition; NMR binding studies; Pseudomonas aeruginosa; Aldose-Ketose Isomerases; Anti-Bacterial Agents; Bacterial Proteins; Drug Design; Enzyme Inhibitors; Escherichia coli; Isomerism; Microbial Sensitivity Tests; Protein Binding; Pseudomonas aeruginosa; Recombinant Proteins; Substrate Specificity; Biochemistry; Clinical Biochemistry; Molecular Biology; Molecular Medicine; Organic Chemistry; Drug Discovery3003 Pharmaceutical Science; 3003; Medicine (all)
Elenco autori:
L. Gabrielli, S. Merlo, C. Airoldi, P. Sperandeo, S. Gianera, A. Polissi, F. Nicotra, T.P. Holler, R.W. Woodard, L. Cipolla
Link alla scheda completa: