Ribose 5-Phosphate Isomerase A (RPIA) is an enzyme encoded by the RPIA gene in humans. This enzyme plays a crucial role in the pentose phosphate pathway, which is essential for cellular metabolism. The enzyme catalyzes the reversible conversion between ribose-5-phosphate (R5P) and ribulose-5-phosphate (Ru5P), facilitating the interconversion of these structural isomers of pentose .
The RPIA gene is located on the short arm (p arm) of the second chromosome at position 11.2. The gene spans nearly 60,000 base pairs and encodes a protein that forms a homodimer consisting of two 25 kDa subunits . The molecular mass of the RPIA dimer is approximately 49 kDa . The enzyme’s structure includes a five-stranded β-sheet surrounded by α-helices, forming an αβα motif .
RPIA is highly conserved across various species, indicating its ancient origins and essential role in metabolism. Knock-out experiments on genes encoding RPIA in different species have shown similar conserved residues and structural motifs . This conservation suggests that the enzyme has been present throughout most of evolutionary history .
RPIA is involved in the pentose phosphate pathway, a metabolic pathway parallel to glycolysis. This pathway generates NADPH and pentoses (5-carbon sugars) as well as ribose-5-phosphate for nucleotide synthesis. The enzyme’s activity is crucial for maintaining cellular redox balance and providing precursors for biosynthetic processes .
RPIA has garnered attention as a potential drug target for treating diseases caused by trypanosomatid parasites, such as Chagas’ disease, leishmaniasis, and human African trypanosomiasis . Additionally, the enzyme’s role in the pentose phosphate pathway makes it a valuable biocatalyst for producing rare sugars, including D-allose, L-rhamnulose, L-lyxose, and L-tagatose .