PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 11179210-1 2001 Dihydropyrimidine dehydrogenase catalyzes the first step in pyrimidine degradation: the NADPH-dependent reduction of uracil and thymine to the corresponding 5,6-dihydropyrimidines. NADP 88-93 dihydropyrimidine dehydrogenase Sus scrofa 0-31 15899693-5 2005 Analysis of the crystal structure of pig DPD suggested that the E244V mutation might interfere with the electron flow between NADPH and the pyrimidine binding site of DPD. NADP 126-131 dihydropyrimidine dehydrogenase Sus scrofa 41-44 18600544-5 2008 Analysis of the crystal structure of pig DPD suggested that the R235Q mutation might interfere with the binding of FAD and the electron flow between the NADPH and the pyrimidine substrate site of DPD. NADP 153-158 dihydropyrimidine dehydrogenase Sus scrofa 41-44 18600544-5 2008 Analysis of the crystal structure of pig DPD suggested that the R235Q mutation might interfere with the binding of FAD and the electron flow between the NADPH and the pyrimidine substrate site of DPD. NADP 153-158 dihydropyrimidine dehydrogenase Sus scrofa 196-199 7575656-2 1995 The assay, which used radiolabeled uracil as a substrate, was validated using recombinant pig DPD in which it was demonstrated to yield kinetic constants similar to those found by methods that rely on either spectroscopic determination of NADPH oxidation or HPLC. NADP 239-244 dihydropyrimidine dehydrogenase Sus scrofa 94-97 20831907-2 2010 Dihydropyrimidine dehydrogenase (DPD) catalyses its first and rate-limiting step, reducing uracil and thymine to the corresponding 5,6-dihydropyrimidines in an NADPH-dependent reaction. NADP 160-165 dihydropyrimidine dehydrogenase Sus scrofa 0-31 20831907-2 2010 Dihydropyrimidine dehydrogenase (DPD) catalyses its first and rate-limiting step, reducing uracil and thymine to the corresponding 5,6-dihydropyrimidines in an NADPH-dependent reaction. NADP 160-165 dihydropyrimidine dehydrogenase Sus scrofa 33-36 15899693-5 2005 Analysis of the crystal structure of pig DPD suggested that the E244V mutation might interfere with the electron flow between NADPH and the pyrimidine binding site of DPD. NADP 126-131 dihydropyrimidine dehydrogenase Sus scrofa 167-170