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Literature summary for 1.3.1.2 extracted from

  • Podschun, B.; Jahnke, K.; Schnackerz, K.D.; Cook, P.F.
    Acid base catalytic mechanism of the dihydropyrimidine dehydrogenase from pH studies (1993), J. Biol. Chem., 268, 3407-3413.
    View publication on PubMed

Application

Application Comment Organism
medicine target for inhibitor design to enhance the cytotoxical effect of 5-fluorouracil in tumor cells by inhibiting the DPD activity with 5-fluorouracil as substrate Sus scrofa

Inhibitors

Inhibitors Comment Organism Structure
5,6-dihydrouracil competitive Sus scrofa
ATP-ribose competitive Sus scrofa

Localization

Localization Comment Organism GeneOntology No. Textmining
cytoplasm
-
Sus scrofa 5737
-

Organism

Organism UniProt Comment Textmining
Sus scrofa
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Sus scrofa

Reaction

Reaction Comment Organism Reaction ID
5,6-dihydrouracil + NADP+ = uracil + NADPH + H+ mechanism, rate-determining half-reaction for reduction of flavin by NADPH has minor rate limitation, while the following protonation of flavin at N-1 is slow Sus scrofa

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
Sus scrofa
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.417 0.5 purified enzyme Sus scrofa

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
thymine + NADPH
-
Sus scrofa dihydrothymine + NADP+
-
?
uracil + NADPH
-
Sus scrofa 5,6-dihydrouracil + NADP+
-
?

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
additional information
-
investigation of pH-dependency of the reaction and inhibition by 2,6-dihydrouracil and ATP-ribose, kinetics Sus scrofa

pH Range

pH Minimum pH Maximum Comment Organism
5.8 8.5
-
Sus scrofa

Cofactor

Cofactor Comment Organism Structure
flavin
-
Sus scrofa
NADPH strictly dependent on Sus scrofa