Dihydropyrimidine dehydrogenase

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Dihydropyrimidine dehydrogenase (DPD) is an enzyme that is involved in pyrimidine degradation. It is the initial and rate-limiting step in pyrimidine catabolism. It catalyzes the reduction of uracil and thymine. It is also involved in the degradation of the chemotherapeutic drug 5-fluorouracil.

[edit] See also

• Dihydropyrimidine dehydrogenase deficiency

[edit] External links

• Online 'Mendelian Inheritance in Man' (OMIM) 274270

• dpd genotype testing (www.mdl-labs.com)

This enzyme-related article is a stub. You can help Wikipedia by expanding it.

v • d • e Metabolism: amino acid metabolism - nucleotide enzymes Purine anabolism synthesis: Amidophosphoribosyltransferase - Inosine monophosphate synthase GMP (IMP dehydrogenase, GMP synthase, GMP reductase) AMP (Adenylosuccinate synthase, Adenylosuccinate lyase, AMP deaminase) Purine catabolism Adenosine deaminase - Purine nucleoside phosphorylase - Guanine deaminase - Xanthine oxidase - Urate oxidase Nucleotide salvage Hypoxanthine-guanine phosphoribosyltransferase - Adenine phosphoribosyltransferase Pyrimidine metabolism CAD (Carbamoyl phosphate synthase II, Aspartate carbamoyltransferase, Dihydroorotase) - Dihydroorotate dehydrogenase - Orotidine 5'-phosphate decarboxylase - CTP synthase - Dihydropyrimidine dehydrogenase Deoxyribonucleotide Ribonucleotide reductase - Nucleoside-diphosphate kinase - DCMP deaminase - Thymidylate synthase - Dihydrofolate reductase see also disorders

Categories: Enzyme stubs

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• This page was last modified 20:53, 9 May 2008 by Wikipedia user Arcadian. Based on work by Wikipedia user(s) Grimgene and Wouterstomp.
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