Dihydroorotate dehydrogenase

Dihydroorotate dehydrogenase (DHODH) is an enzyme that plays a crucial role in the de novo synthesis of pyrimidines in humans. It catalyzes the fourth step in the process, converting dihydroorotate to orotate.

Function

DHODH is located on the outer surface of the inner mitochondrial membrane, where it is involved in the electron transport chain. It is a flavoprotein that uses ubiquinone as an electron acceptor, which is then reduced to ubiquinol. This process is essential for the production of UMP, the precursor to all pyrimidine nucleotides.

Clinical significance

Mutations in the DHODH gene have been associated with Miller syndrome, a rare autosomal recessive disorder characterized by postaxial acrofacial dysostosis. In addition, inhibitors of DHODH have been used as immunosuppressive and antiproliferative agents. For example, leflunomide, a drug used to treat rheumatoid arthritis, inhibits DHODH, thereby reducing the synthesis of pyrimidines and suppressing the immune response.

See also

• Pyrimidine biosynthesis
• Miller syndrome
• Leflunomide

External links

• DHODH at GeneCards
• DHODH at UniProt

Dihydroorotate dehydrogenase Resources
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