Sandbox Reserved 315: Difference between revisions

'''Orotidine monophosphate decarboxylase''' (ODCase), also known as '''orotidine 5’-monophosphate decarboxylase''' (OMP decarboxylase) or '''orotidine 5’-phosphate decarboxylase''' is an enzyme involved in pyrimidine biosynthesis. It catalyzes the conversion of orotidine 5’-monophosphate (OMP) to uridine 5’-monophosphate (UMP). This reaction is the final step in de novo pyrimidine nucleotide synthesis and is an essential precursor for both DNA and RNA. The main structure of orotidine monophosphate decarboxylase is a TIM barrel, with one side acting as the binding site, while the other side is closed-off. ODCase is often bound to other proteins in biological conditions. In single-cellular organisms, it can form a dimeric enzyme by binding to another ODCase<ref name = "Wu"/>. In multi-cellular organisms it can bind to orotate phosphoribosyltransferase to form a bifunctional protein<ref name = "Yablonski"/>. Additionally this enzyme has been studied for it’s remarkable catalytic efficiency.<Ref name = "Miller">PMID:10681417</ref>.