Phosphopentose epimerase (also known as ribulose-phosphate 3-epimerase and ribulose 5-phosphate 3-epimerase, EC5.1.3.1) encoded in humans by the RPE gene[1] is a metalloprotein that catalyzes the interconversion between D-ribulose 5-phosphate and D-xylulose 5-phosphate.[2]
D-ribulose 5-phosphate D-xylulose 5-phosphate
This reversible conversion is required for carbon fixation in plants – through the Calvin cycle – and for the nonoxidative phase of the pentose phosphate pathway.[3][4] This enzyme has also been implicated in additional pentose and glucuronate interconversions.
In Cupriavidus metallidurans two copies of the gene coding for PPE are known,[5] one is chromosomally encoded P40117, the other one is on a plasmid Q04539. PPE has been found in a wide range of bacteria, archaebacteria, fungi and plants. All the proteins have from 209 to 241 amino acid residues. The enzyme has a TIM barrel structure.