UMPS Human
OPRT, Uridine 5'-monophosphate synthase, UMP synthase, Orotate phosphoribosyltransferase , OPRT, OPRTase, Orotidine 5'-phosphate decarboxylase , ODC, OMPdecase.
Description
Product Specs
OPRT, Uridine 5'-monophosphate synthase, UMP synthase, Orotate phosphoribosyltransferase , OPRT, OPRTase, Orotidine 5'-phosphate decarboxylase , ODC, OMPdecase.
Product Science Overview
UMPS is composed of two distinct enzymatic domains:
- Orotate Phosphoribosyltransferase (OPRTase): This domain catalyzes the transfer of a ribose-phosphate group to orotate, forming orotidine-5’-monophosphate (OMP).
- Orotidine-5’-Phosphate Decarboxylase (ODCase): This domain decarboxylates OMP to form UMP.
In humans, these two domains are fused into a single polypeptide chain, enhancing the enzyme’s stability and efficiency . The gene encoding UMPS is located on the long arm of chromosome 3 (3q13) .
The human recombinant UMPS is produced by cloning the UMPS gene into an expression vector, which is then introduced into E. coli cells. These cells are cultured under conditions that promote the expression of the UMPS protein. The recombinant protein is then purified using chromatographic techniques to obtain a high-purity product .
UMPS is vital for the synthesis of pyrimidine nucleotides, which are essential for various cellular processes, including:
- DNA and RNA synthesis: UMP serves as a precursor for the synthesis of other pyrimidine nucleotides, such as cytidine triphosphate (CTP) and thymidine triphosphate (TTP).
- Cellular metabolism: Pyrimidine nucleotides are involved in energy metabolism and the regulation of various enzymatic reactions.
Mutations in the UMPS gene can lead to a rare metabolic disorder known as orotic aciduria. This condition is characterized by an accumulation of orotic acid in the urine, leading to developmental delays, megaloblastic anemia, and immune deficiencies . Recombinant UMPS can be used in research to study the enzyme’s function and to develop potential therapies for orotic aciduria.
