Recombinant Human OPRT protein (His tag) is a Human Full Length protein, in the 1 to 480 aa range, expressed in Baculovirus infected insect, with >95% purity, < 1 EU/µg endotoxin level and suitable for SDS-PAGE.
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Bifunctional enzyme catalyzing the last two steps of de novo pyrimidine biosynthesis, orotate phosphoribosyltransferase (OPRT), which converts orotate to orotidine-5'-monophosphate (OMP), and orotidine-5'-monophosphate decarboxylase (ODC), the terminal enzymatic reaction that decarboxylates OMP to uridine monophosphate (UMP).
OK/SW-cl.21, UMPS, Uridine 5'-monophosphate synthase, UMP synthase
Recombinant Human OPRT protein (His tag) is a Human Full Length protein, in the 1 to 480 aa range, expressed in Baculovirus infected insect, with >95% purity, < 1 EU/µg endotoxin level and suitable for SDS-PAGE.
pH: 7.4
Constituents: PBS
Affinity purified
Bifunctional enzyme catalyzing the last two steps of de novo pyrimidine biosynthesis, orotate phosphoribosyltransferase (OPRT), which converts orotate to orotidine-5'-monophosphate (OMP), and orotidine-5'-monophosphate decarboxylase (ODC), the terminal enzymatic reaction that decarboxylates OMP to uridine monophosphate (UMP).
In the N-terminal section; belongs to the purine/pyrimidine phosphoribosyltransferase family.
This product was previously labelled as UMPS
Orotate phosphoribosyltransferase often abbreviated as OPRT or known by its enzyme commission number EC 2.4.2.10 plays a significant role in pyrimidine biosynthesis. This enzyme with a molecular weight of around 23 kDa catalyzes the conversion of orotate and 5-phosphoribosyl-1-pyrophosphate (PRPP) into orotidine-5'-monophosphate (OMP). OPRT is expressed in various tissues with notably higher levels in rapidly proliferating cells due to their increased demand for nucleotides.
Orotate phosphoribosyltransferase contributes to the de novo synthesis of pyrimidine nucleotides which are essential components of DNA and RNA. OPRT operates as part of the UMP biosynthesis via the de novo pathway forming a complex with orotidine-5'-phosphate decarboxylase in some organisms. This linkage enhances efficiency in pyrimidine nucleotide production reflecting its central role in cell growth and division.
The protein integrates into the pyrimidine metabolism pathway. It interacts closely with orotate phosphoribosyltransferase and orotidine-5'-phosphate decarboxylase forming dual-function enzymes that streamline UMP synthesis. OPRT’s activity ties it to key metabolic cycles including nucleotide salvage pathways thereby establishing critical links across metabolic networks essential for nucleic acid production.
Dysfunction in Orotate phosphoribosyltransferase can lead to hereditary orotic aciduria a rare autosomal recessive disorder characterized by megaloblastic anemia and excessive orotate excretion. Changes in OPRT activity also impact pyrimidine antimetabolite drug efficacy such as 5-fluorouracil demonstrating its significance in cancer treatment. Additionally OPRT's interactions with dihydroorotate dehydrogenase can be important in understanding metabolic disturbances related to pyrimidine disorders.
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15% SDS-PAGE analysis of 3 μg ab226883.
MW: 50-70 kDa (SDS-PAGE under reducing conditions).
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