Conformations of nicotinamide coenzymes bound to dehydrogenases determined by transferred nuclear Overhauser effects.
Transferred nuclear Overhauser enhancement was used to examine the conformation of NAD+ and NADP+ bound to glucose-6-phosphate dehydrogenase and glutamate dehydrogenase and of NAD+ bound to lactate dehydrogenase. The results demonstrate that the conformation of the nicotinamide-ribose bond is anti for dehydrogenases with A stereospecificity and syn for dehydrogenases with B stereospecificity. In those dehydrogenases that bind both NAD+ and NADP+, significant differences occur in the conformations of the bound nicotinamide coenzymes.
D000818:Animals; D002417:Cattle; D005954:Glucosephosphate Dehydrogenase / Q000378:metabolism*; D005969:Glutamate Dehydrogenase / Q000378:metabolism*; D007770:L-Lactate Dehydrogenase / Q000378:metabolism*; D007934:Leuconostoc / Q000201:enzymology; D008099:Liver / Q000201:enzymology; D008968:Molecular Conformation; D009206:Myocardium / Q000201:enzymology; D009243:NAD / Q000378:metabolism*; D009249:NADP / Q000378:metabolism*; D011485:Protein Binding; D051381:Rats
D009243:NAD; D009249:NADP; D007770:L-Lactate Dehydrogenase; D005954:Glucosephosphate Dehydrogenase; D005969:Glutamate Dehydrogenase