Hydride transfer stereospecificity of rat liver aldehyde dehydrogenases.
The stereospecificity of hydride transfer to NAD+ by several forms of rat liver aldehyde dehydrogenase was determined by a nuclear magnetic resonance method. The forms included several mitochondrial and microsomal isozymes from normal liver, as well as isozymes from xenobiotic-treated and tumor cells. The proton added to NAD+ comes exclusively from the aldehyde substrate and in all cases was A (pro-R)-stereospecific.
D000444:Aldehyde Dehydrogenase / Q000378:metabolism*; D000818:Animals; D007527:Isoenzymes / Q000378:metabolism*; D008099:Liver / Q000187:drug effects / Q000201:enzymology*; D008114:Liver Neoplasms, Experimental / Q000201:enzymology; D009682:Magnetic Resonance Spectroscopy; D008862:Microsomes, Liver / Q000201:enzymology; D008930:Mitochondria, Liver / Q000201:enzymology; D008968:Molecular Conformation; D009243:NAD / Q000378:metabolism; D010634:Phenobarbital / Q000494:pharmacology; D000072317:Polychlorinated Dibenzodioxins / Q000494:pharmacology; D011522:Protons; D051381:Rats
D007527:Isoenzymes; D000072317:Polychlorinated Dibenzodioxins; D011522:Protons; D009243:NAD; D000444:Aldehyde Dehydrogenase; D010634:Phenobarbital