Stereochemistry of NADPH oxidation by dihydropyrimidine dehydrogenase from pig liver.
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.
Podschun
B
B
Theodor-Boveri-Institut fuer Biowissenschaften (Biozentrum), Universitaet Wuerzburg, Germany.
D000818:Animals; D003600:Cytosol / Q000201:enzymology; D003903:Deuterium; D042943:Dihydrouracil Dehydrogenase (NADP); D007700:Kinetics; D008099:Liver / Q000201:enzymology*; D009682:Magnetic Resonance Spectroscopy; D015394:Molecular Structure; D009249:NADP / Q000737:chemistry / Q000378:metabolism*; D010084:Oxidation-Reduction; D010088:Oxidoreductases / Q000378:metabolism*; D011865:Radioisotope Dilution Technique; D013237:Stereoisomerism; D013552:Swine; D014498:Uracil / Q000737:chemistry / Q000378:metabolism
D009249:NADP; D014498:Uracil; D003903:Deuterium; D010088:Oxidoreductases; D042943:Dihydrouracil Dehydrogenase (NADP)