The stereospecificity of oxidation of alpha-[4R-2H]NADH by dehydrogenases.
The stereospecificity of the enzyme-dependent oxidation of alpha-[4R-2H]NADH has been determined for four dehydrogenases: two pro-R specific enzymes, pig heart malate dehydrogenase and yeast alcohol dehydrogenase; and two pro-S specific enzymes, rabbit muscle glycerol-3-phosphate dehydrogenase and Rhodopseudomonas spheroides 3-hydroxybutyrate dehydrogenase. In all cases, an enzyme-dependent and substrate-specific oxidation to alpha-NAD+ is observed with the stereochemistry of oxidation identical with that found for the oxidation of the correspondingly labeled beta-NADH. The ability of dehydrogenases from diverse sources to utilize alpha-NADH in a stereochemically competent fashion is discussed in relation to proposed interactions between the nicotinamide sugar moiety and active site residues or obligatory alignments of the pyridine and sugar moieties.
D000426:Alcohol Dehydrogenase; D000429:Alcohol Oxidoreductases / Q000378:metabolism; D000818:Animals; D005993:Glycerolphosphate Dehydrogenase / Q000378:metabolism; D006884:Hydroxybutyrate Dehydrogenase / Q000378:metabolism; D009682:Magnetic Resonance Spectroscopy; D008291:Malate Dehydrogenase / Q000378:metabolism; D009206:Myocardium / Q000201:enzymology; D009243:NAD / Q000378:metabolism*; D010088:Oxidoreductases / Q000378:metabolism*; D011817:Rabbits; D013237:Stereoisomerism; D013552:Swine; D015003:Yeasts / Q000201:enzymology
D009243:NAD; D010088:Oxidoreductases; D000429:Alcohol Oxidoreductases; D005993:Glycerolphosphate Dehydrogenase; D000426:Alcohol Dehydrogenase; D006884:Hydroxybutyrate Dehydrogenase; D008291:Malate Dehydrogenase