title: Modifications around the hydroxamic acid chelating group of fosmidomycin, an inhibitor of the metalloenzyme 1-deoxyxylulose 5-phosphate reductoisomerase (DXR).
abstract: Fosmidomycin derivatives in which the hydroxamic acid group has been replaced by several bidentate chelators as potential hydroxamic alternatives were prepared and tested against the DXR from Escherichia coli. These results illustrate the predominant role of the hydroxamate functional group as the most effective metal binding group in DXR inhibitors.
authors.affiliation: Université de Strasbourg/CNRS, Strasbourg, UMR 7177, Institut Le Bel, 4 rue Blaise Pascal 67081, Strasbourg, France.
authors.forename: Catherine
authors.initials: C
authors.lastname: Zinglé
authors.forename: Lionel
authors.initials: L
authors.lastname: Kuntz
authors.forename: Denis
authors.initials: D
authors.lastname: Tritsch
authors.forename: Catherine
authors.initials: C
authors.lastname: Grosdemange-Billiard
authors.forename: Michel
authors.initials: M
authors.lastname: Rohmer
mesh_terms: D019747:Aldose-Ketose Isomerases / Q000037:antagonists & inhibitors / Q000737:chemistry*; D002614:Chelating Agents / Q000737:chemistry* / Q000494:pharmacology; D004789:Enzyme Activation / Q000187:drug effects; D004791:Enzyme Inhibitors / Q000737:chemistry* / Q000494:pharmacology; D004926:Escherichia coli / Q000201:enzymology; D005578:Fosfomycin / Q000031:analogs & derivatives* / Q000737:chemistry / Q000494:pharmacology; D006877:Hydroxamic Acids / Q000737:chemistry*; D020128:Inhibitory Concentration 50; D008667:Metalloproteins / Q000737:chemistry; D015394:Molecular Structure; D011485:Protein Binding / Q000187:drug effects
chemical_list: D002614:Chelating Agents; D004791:Enzyme Inhibitors; D006877:Hydroxamic Acids; D008667:Metalloproteins; D005578:Fosfomycin; C024640:fosmidomycin; C114231:1-deoxy-D-xylulose 5-phosphate reductoisomerase; D019747:Aldose-Ketose Isomerases