Pyrimidine biosynthesis enzyme

Pyrimidine biosynthesis enzymes are a group of metabolic enzymes that catalyze the de novo synthesis of pyrimidine nucleotides, essential precursors for DNA and RNA synthesis in all proliferating cells. The pathway primarily involves the enzymes carbamoyl phosphate synthetase II (CPS II), aspartate transcarbamoylase, dihydroorotase, dihydroorotate dehydrogenase (DHODH), orotate phosphoribosyltransferase, and orotidine 5’-monophosphate decarboxylase. In mammals, the first three enzymatic steps are carried out by a single multifunctional enzyme known as CAD. These enzymes are tightly regulated through feedback and allosteric mechanisms to control nucleotide supply and cellular proliferation. Inhibitors of this pathway, especially DHODH inhibitors such as leflunomide and teriflunomide, are clinically used to treat autoimmune diseases and are under investigation for cancer therapy. Overactivity or dysregulation of pyrimidine biosynthesis is associated with malignancy, and genetic deficiencies can result in developmental disorders. The target entry "Pyrimidine biosynthesis enzymes" is too broad as it refers to a class of enzymes, not a single canonical target. For structured data, it is best to specify individual enzymes (e.g., dihydroorotate dehydrogenase [DHODH], CAD, CTP synthase), each of which has distinct properties, functions, inhibitors, and clinical roles.

Other names

Pyrimidine biosynthetic enzymePyrimidine synthesis enzymeEnzymes of pyrimidine biosynthesis

Inhibition of dihydroorotate dehydrogenase (e.g., Leflunomide, Teriflunomide, Brequinar); Inhibition of de novo pyrimidine synthesis to suppress DNA/RNA production and cell proliferation