Biophysical tools to monitor enzyme-ligand interactions of enzymes involved in vitamin biosynthesis.
Knowledge of biomolecular interactions is of importance to our understanding of biological processes such as enzyme catalysis and inhibition. Biophysical techniques enable sensitive detection and accurate characterization of binding and are therefore powerful tools in enzymology and rational drug design. The applications of NMR spectroscopy and isothermal titration calorimetry to study enzyme-ligand interactions will be discussed. Recent work on ketopantoate reductase, which catalyses an important step on the biosynthetic pathway to vitamin B5, is used to illustrate the potential of this approach.
Ciulli
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University Chemical Laboratory, Lensfield Road, Cambridge CB2 1EW, UK. ac313@cam.ac.uk
Abell
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D000429:Alcohol Oxidoreductases / Q000737:chemistry / Q000378:metabolism; D001419:Bacteria / Q000201:enzymology; D002151:Calorimetry; D004798:Enzymes / Q000378:metabolism*; D005658:Fungi / Q000201:enzymology; D007700:Kinetics; D008024:Ligands; D009682:Magnetic Resonance Spectroscopy; D008954:Models, Biological; D010944:Plants / Q000201:enzymology; D014815:Vitamins / Q000096:biosynthesis*
D004798:Enzymes; D008024:Ligands; D014815:Vitamins; D000429:Alcohol Oxidoreductases; C021934:2-dehydropantoate 2-reductase