In enzymology, a phosphopentomutase () is an enzyme that catalyzes the chemical reaction
alpha-D-ribose 1-phosphate D-ribose 5-phosphate
Hence, this enzyme has one substrate, alpha-D-ribose 1-phosphate, and one product, D-ribose 5-phosphate.
This enzyme belongs to the family of isomerases, specifically the phosphotransferases (phosphomutases), which transfer phosphate groups within a molecule. The systematic name of this enzyme class is alpha-D-ribose 1,5-phosphomutase. Other names in common use include phosphodeoxyribomutase, deoxyribose phosphomutase, deoxyribomutase, phosphoribomutase, alpha-D-glucose-1,6-bisphosphate:deoxy-D-ribose-1-phosphate, phosphotransferase, and D-ribose 1,5-phosphomutase. This enzyme participates in pentose phosphate pathway and purine metabolism. It has 3 cofactors: D-ribose 1,5-bisphosphate, alpha-D-Glucose 1,6-bisphosphate, and 2-Deoxy-D-ribose 1,5-bisphosphate.
Structural studies
The first published description of a structure of a prokaryotic phosphopentomutase was in 2011.Panosian, T. D., Nanneman, D. P., Watkins, G, Phalen V. V., McDonald W.H., Wadzinski B. E., Bachmann B. O., Iverson T.M. 2011. Bacillus cereus phosphopentomtuase is an alkaline phosphatase family member with an altered entry point into the catalytic cycle. J. Biol. Chem. 286 (8043-8054). Structures of Bacillus cereus phosphopentomutase as it was purified, after activation, bound to ribose 5-phosphate and bound to glucose 1,6-bisphosphate are deposited in the PDB with accession codes , , and , respectively.
References
Boyer, P.D. (Ed.), The Enzymes, 3rd ed., vol. 6, 1972, p. 407-477.