Stereochemistry of NADPH oxidation by dihydropyrimidine dehydrogenase from pig liver

Biochem Biophys Res Commun. 1992 Jan 31;182(2):609-16. doi: 10.1016/0006-291x(92)91776-m.

Abstract

Dihydropyrimidine dehydrogenase reduces uracil to 5,6-dihydrouracil in a strictly NADPH-dependent reaction. Either by analysing the 1H-NMR spectra of the NADP+ products formed or by determination of the kinetic isotope effects of stereospecifically deuterated coenzymes dihydropyrimidine dehydrogenase was found to abstract specifically the pro-S hydrogen of NADPH, making it a member of the B-side stereospecific class of dehydrogenases.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cytosol / enzymology
  • Deuterium
  • Dihydrouracil Dehydrogenase (NADP)
  • Kinetics
  • Liver / enzymology*
  • Magnetic Resonance Spectroscopy
  • Molecular Structure
  • NADP / chemistry
  • NADP / metabolism*
  • Oxidation-Reduction
  • Oxidoreductases / metabolism*
  • Radioisotope Dilution Technique
  • Stereoisomerism
  • Swine
  • Uracil / chemistry
  • Uracil / metabolism

Substances

  • NADP
  • Uracil
  • Deuterium
  • Oxidoreductases
  • Dihydrouracil Dehydrogenase (NADP)