| phosphopentomutase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 5.4.2.7 | ||||||||
| CAS no. | 9026-77-1 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
In enzymology, a phosphopentomutase ( EC 5.4.2.7) 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. [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).Panosian, Timothy D.; Nannemann, David P.; Watkins, Guy R.; Phelan, Vanessa V.; McDonald, W. Hayes; Wadzinski, Brian E.; Bachmann, Brian O.; Iverson, Tina M. (March 2011). "Bacillus cereus phosphopentomutase is an alkaline phosphatase family member that exhibits an altered entry point into the catalytic cycle". Journal of Biological Chemistry. 286 (10): 8043–54. doi: 10.1074/jbc.M110.201350. PMC 3048691. 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. doi: 10.1016/S0021-9258(18)94286-9. PMID 5824563.
- Boyer, P.D. (Ed.), The Enzymes, 3rd ed., vol. 6, 1972, p. 407-477.
| phosphopentomutase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 5.4.2.7 | ||||||||
| CAS no. | 9026-77-1 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
In enzymology, a phosphopentomutase ( EC 5.4.2.7) 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. [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).Panosian, Timothy D.; Nannemann, David P.; Watkins, Guy R.; Phelan, Vanessa V.; McDonald, W. Hayes; Wadzinski, Brian E.; Bachmann, Brian O.; Iverson, Tina M. (March 2011). "Bacillus cereus phosphopentomutase is an alkaline phosphatase family member that exhibits an altered entry point into the catalytic cycle". Journal of Biological Chemistry. 286 (10): 8043–54. doi: 10.1074/jbc.M110.201350. PMC 3048691. 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. doi: 10.1016/S0021-9258(18)94286-9. PMID 5824563.
- Boyer, P.D. (Ed.), The Enzymes, 3rd ed., vol. 6, 1972, p. 407-477.