In enzymology, a phosphopentomutase (EC 5.4.2.7) is an enzyme that catalyzes the chemical reaction
alpha-D-ribose 1-phosphate ⇌ {\displaystyle \rightleftharpoons } 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. 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 PDB: 3M8W, PDB: 3M8Y, PDB: 3M8Z and PDB: 3OT9, respectively.
References
Hammer-Jespersen K, Munch-Petersen A (1970). "Phosphodeoxyribomutase from Escherichia coli. Purification and some properties". Eur. J. Biochem. 17 (3): 397–407. doi:10.1111/j.1432-1033.1970.tb01179.x. PMID 4992818. Kammen HO, Koo R (1969). "Phosphopentomutases. I. Identification of two activities in rabbit tissues". J. Biol. Chem. 244 (18): 4888–93. doi:10.1016/S0021-9258(18)94286-9. PMID 5824563. Boyer, P.D. (Ed.), The Enzymes, 3rd ed., vol. 6, 1972, p. 407-477.
