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Target intelligence / Profile preview
Dihydropyrimidine dehydrogenase
- Molecular classification
- Enzyme
01
Overview
Dihydropyrimidine dehydrogenase (DPD) is a key enzyme involved in the catabolism of pyrimidines, specifically uracil and thymine. It catalyzes the initial and rate-limiting step in their breakdown, converting uracil to 5,6-dihydrouracil and thymine to 5,6-dihydrothymine. Over 80% of administered fluoropyrimidine drugs (such as 5-fluorouracil [5-FU] and its prodrug capecitabine) are metabolized by DPD into inactive metabolites. Deficient DPD activity leads to severe side effects when treated with fluoropyrimidines.
- Other names
- Dihydrothymine dehydrogenase
02
Mechanism of action
Metabolizes fluoropyrimidine drugs (such as 5-fluorouracil [5-FU] and its prodrug capecitabine) into inactive metabolites.
03
Biological functions
Pyrimidines catabolismDrug metabolism
04
Disease associations
Dihydropyrimidine Dehydrogenase DeficiencyNeurological disordersDevelopmental delaysChemotherapy toxicity
05
Safety considerations
Severe toxicity (hematologic, gastrointestinal, dermatologic) from fluoropyrimidine drugs in patients with DPD deficiencyNeurological and developmental issues in patients with complete DPD deficiency
06
Interacting drugs
5-Fluorouracil (5-FU)
1 more in the full profile.
07
Biomarkers
DPYD variants (e.g., c.1905+1G>A, c.299_302del, c.703C>T, c.2983G>T, c.1679T>G) for predicting fluoropyrimidine toxicity
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