Recombinant Human DPD protein (GST tag N-Terminus)

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

DPD also known as dihydropyrimidine dehydrogenase is an enzyme important for the breakdown of pyrimidines particularly uracil and thymine. The DPD protein has an important role in the initial step of pyrimidine catabolism. It catalyzes the NADPH-dependent reduction of these pyrimidines to dihydrouracil and dihydrothymine. It consists of 1025 amino acids giving it a mass of approximately 111 kDa. DPD is expressed in various tissues with significant expression in the liver and to a lesser extent in peripheral blood lymphocytes.

Biological function summary

Dihydropyrimidine dehydrogenase impacts nucleotide metabolism which is significant for cellular replication and repair processes. DPD exists as part of a multi-enzyme complex that handles pyrimidine metabolism. It serves an important regulatory function by controlling the level of pyrimidines within cells. This regulation keeps the balance of free nucleotides which is critical for DNA synthesis and overall cellular homeostasis.

Pathways

DPD holds an important position in pyrimidine metabolism pathways and the drug metabolism pathway specifically influencing fluoropyrimidine-based chemotherapeutic agents. Within the pyrimidine metabolic pathway DPD links to other enzymes that further breakdown pyrimidines into more basic compounds. In drug metabolism DPD plays a vital role by metabolizing drugs like 5-fluorouracil. Its activity affects how individuals process these medications linking it to enzymes like thymidylate synthase that share pathways in cancer treatment drug action.

DPD deficiency relates to a genetic disorder that causes an excessive build-up of uracil and thymine leading to developmental disorders and neurological problems. Additionally abnormalities in DPD activity influence the efficacy and toxicity of fluorouracil chemotherapy in cancer treatments. DPD enzymatic activity when not properly regulated can lead to severe toxic reactions especially in relation to therapies reliant on enzymes such as thymidylate synthase emphasizing the critical interplay between these proteins in the management of fluoropyrimidine drug treatments.