UPP1 E.coli

Uridine Phosphorylase is found in various organisms, including bacteria like Escherichia coli (E. coli). In E. coli, the enzyme is encoded by the upp gene. The primary function of UPP in E. coli is to facilitate the utilization of uridine and deoxyuridine as carbon and energy sources. Additionally, it plays a role in the rescue of pyrimidine bases for nucleotide synthesis .

Recombinant Uridine Phosphorylase from E. coli is produced by cloning the upp gene into an expression vector, which is then introduced into an E. coli host strain. The recombinant protein is typically fused with a His-tag at the N-terminus to facilitate purification. The protein is expressed in E. coli and purified using conventional chromatography techniques .

The recombinant E. coli Uridine Phosphorylase has a molecular weight of approximately 29.3 kDa. It exhibits high specific activity, with the ability to catalyze the reduction of uridine in the presence of phosphate at a rate of over 20,000 pmol/min/µg at pH 7.5 and 25°C . The enzyme’s activity is crucial for maintaining uridine homeostasis and supporting the pyrimidine salvage pathway.

Recombinant Uridine Phosphorylase from E. coli is used in various research applications, including:

• Biochemical studies: Understanding the enzyme’s mechanism and kinetics.
• Drug development: Investigating potential inhibitors for therapeutic purposes, particularly in the context of pyrimidine-based chemotherapeutic compounds like 5-fluorouracil (5-FU) and its prodrug capecitabine .
• Biotechnology: Utilizing the enzyme in synthetic biology and metabolic engineering to enhance nucleotide synthesis pathways.