Orotidine 5'-phosphate decarboxylase
（重定向自OMP decarboxylase）
![](/Images/godic/202501/31/OMP_decarboxylase2716.png")
![Schematic of reaction catalyzed by OMP decarboxylase](/Images/godic/202501/31/OMPDC_Reaction2716.png")
![Image representing the structure of the active site of OMP decarboxylase when bound to the inhibitor BMP. Note the Lys and Asp residues surrounding the 6-hydroxyl of the substrate. (Image captured from pymol viewer snapshot of 1LOR crystal structure)[5]](/Images/godic/202501/31/BMP_Bound_to_the_Active_Site_of_OMP_Carboxylase_from_M_thermoautotrophicum2717.png")
![Reaction schematic showing the mechanism of OMP decarboxylase catalysis through a putative vinyl carbanion at the C6 position. This carbanion is likely stabilized by the nearby protonated lysine residue. The Lys93 and Asp91 residue numbering corresponds to the sequence for OMP decarboxylase from S cerevisiae.[13]](/Images/godic/202501/31/OMPDC_Carbanion_Mechanism2717.png")
Orotidine 5’-phosphate decarboxylase (OMP decarboxylase) or orotidylate decarboxylase is an enzyme involved in pyrimidine biosynthesis. It catalyzes the decarboxylation of orotidine monophosphate (OMP) to form uridine monophosphate (UMP). The function of this enzyme is essential to the de novo biosynthesis of the pyrimidine nucleotides uridine triphosphate, cytidine triphosphate, and thymidine triphosphate. OMP decarboxylase has been a frequent target for scientific investigation because of its demonstrated extreme catalytic efficiency and its usefulness as a selection marker for yeast strain engineering.