<unk>  catalyzes the reversible phosphorylation of<unk> , deoxyuridine, and their analogs (except deoxycytidine) to their respective bases (thymine/uracil) and 2-deoxyribose 1-phosphate. The enzyme follows a sequential mechanism, where phosphate binds before<unk>  (or deoxyuridine, etc.) and 2-deoxyribose 1-phosphate leaves after the nitrogenous base. The<unk>  is bound in a high-energy conformation, in which the glycosidic bond weakens as the phosphate attacks the C1 position of the ribose ring, as shown below. The enzyme can then transfer deoxyribose 1-phosphate to other nitrogenous bases.<unk>  mechanism Further experiments have shown that thymine inhibits the enzyme via both substrate inhibition and nonlinear product inhibition. This suggests that thymine can inhibit the enzyme via multiple sites. The enzyme also displays cooperativity with respect to both<unk>  and phosphate in the presence of thymine, which suggests that<unk>  has several allosteric and/or catalytic sites as well.
Thymidine phosphorylase
Xanthine oxidase
Asparaginase
Galactose-1-phosphate uridylyltransferase
Dispase
Iduronate-2-sulfatase
Transaminase
Biotinidase