Phosphopentose epimerase

ribulose-phosphate 3-epimerase
D-ribulose-5-phosphate 3-epimerase dodekamer, Francisella tularensis
Identifiers
EC no.5.1.3.1
CAS no.9024-20-8
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins
Ribulose-phosphate 3 epimerase family
Identifiers
SymbolRibul_P_3_epim
PfamPF00834
InterProIPR000056
PROSITEPDOC00833
SCOP21rpx / SCOPe / SUPFAM
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
PDB1tqjB:6-208 1rpxA:58-260 1h1zA:8-208 1h1yB:8-208 1tqxA:7-208

Phosphopentose epimerase (also known as ribulose-phosphate 3-epimerase and ribulose 5-phosphate 3-epimerase, EC 5.1.3.1) encoded in humans by the RPE gene is a metalloprotein that catalyzes the interconversion between D-ribulose 5-phosphate and D-xylulose 5-phosphate.

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. 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, 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.