Hydride transfer stereospecificity of rat liver aldehyde dehydrogenases.

@article{Jones1987HydrideTS,
  title={Hydride transfer stereospecificity of rat liver aldehyde dehydrogenases.},
  author={Kenneth H. Jones and Ronald Lindahl and David C. Baker and Russell Timkovich},
  journal={The Journal of biological chemistry},
  year={1987},
  volume={262 23},
  pages={
          10911-3
        }
}
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.