Phosphopentomutase

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.^[1] 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 3M8W, 3M8Y, 3M8Z and 3OT9, respectively.

References

↑ 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)."Bacillus cereus phosphopentomutase is an alkaline phosphatase family member that exhibits an altered entry point into the catalytic cycle" 286 (10). March 2011: 8043–54. doi:10.1074/jbc.M110.201350. PMID 21193409.

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. PMID 5824563.
Boyer, P.D. (Ed.), The Enzymes, 3rd ed., vol. 6, 1972, p. 407-477.

Isomerase: mutases (EC 5.4)

5.4.1 Acyl Groups	Lysolecithin acylmutase Precorrin-8X methylmutase

5.4.2 Phosphomutases	Phosphoglycerate mutase Bisphosphoglycerate mutase Phosphoglucomutase Phosphomannomutase PMM1 PMM2

5.4.99 Other groups	Methylmalonyl-CoA mutase Lanosterol synthase

Proteins: enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases(list) EC2 Transferases(list) EC3 Hydrolases(list) EC4 Lyases(list) EC5 Isomerases(list) EC6 Ligases(list)

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