phosphopentomutase

{{infobox enzyme

| Name = phosphopentomutase

| EC_number = 5.4.2.7

| CAS_number = 9026-77-1

| GO_code = 0008973

| image =

| width =

| caption =

}}

In enzymology, a phosphopentomutase ({{EnzExplorer|5.4.2.7}}) is an enzyme that catalyzes the chemical reaction

:alpha-D-ribose 1-phosphate $\rightleftharpoons$ 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.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).{{cite journal|pmid=21193409 | doi=10.1074/jbc.M110.201350 | volume=286 | issue=10 | title=Bacillus cereus phosphopentomutase is an alkaline phosphatase family member that exhibits an altered entry point into the catalytic cycle |date=March 2011 | pages=8043–54|pmc=3048691 | last1=Panosian | first1=Timothy D. | last2=Nannemann | first2=David P. | last3=Watkins | first3=Guy R. | last4=Phelan | first4=Vanessa V. | last5=McDonald | first5=W. Hayes | last6=Wadzinski | first6=Brian E. | last7=Bachmann | first7=Brian O. | last8=Iverson | first8=Tina M. | journal=Journal of Biological Chemistry | doi-access=free }} 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 link|3M8W}}, {{PDB link|3M8Y}}, {{PDB link|3M8Z}} and {{PDB link|3OT9}}, respectively.

References

{{cite journal | vauthors = Hammer-Jespersen K, Munch-Petersen A | year = 1970 | title = Phosphodeoxyribomutase from Escherichia coli. Purification and some properties | journal = Eur. J. Biochem. | volume = 17 | pages = 397–407 | pmid = 4992818 | doi = 10.1111/j.1432-1033.1970.tb01179.x | issue = 3 | doi-access = free }}
{{cite journal | vauthors = Kammen HO, Koo R | year = 1969 | title = Phosphopentomutases. I. Identification of two activities in rabbit tissues | journal = J. Biol. Chem. | volume = 244 | pages = 4888–93 | pmid = 5824563 | issue = 18 | doi = 10.1016/S0021-9258(18)94286-9 | doi-access = free }}
Boyer, P.D. (Ed.), The Enzymes, 3rd ed., vol. 6, 1972, p. 407-477.

Category:EC 5.4.2

Category:Enzymes of known structure