| Identifiers | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| EC no. | 5.4.2.10 | ||||||||
| 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 phosphoglucosamine mutase ( EC 5.4.2.10) is an enzyme that catalyzes the chemical reaction
- alpha-D-glucosamine 1-phosphate D-glucosamine 6-phosphate
Hence, this enzyme has one substrate, alpha-D-glucosamine 1-phosphate, and one product, D-glucosamine 6-phosphate.
This enzyme belongs to the family of isomerases, specifically the phosphotransferases ( α-D-phosphohexomutases), which transfer phosphate groups within a molecule. The systematic name of this enzyme class is alpha-D-glucosamine 1,6-phosphomutase. This enzyme participates in aminosugars metabolism.
Crystal structures of two bacterial phosphoglucosamine mutases are known (PDB entries 3I3W and 3PDK), from Francisella tularensis and Bacillus anthracis. Both share a similar dimeric quaternary structure, as well as conserved features of the active site, as found their enzyme superfamily, the α-D-phosphohexomutases.
References
- Mengin-Lecreulx D, van Heijenoort J (1996). "Characterization of the essential gene glmM encoding phosphoglucosamine mutase in Escherichia coli". J. Biol. Chem. 271 (1): 32–9. doi: 10.1074/jbc.271.1.32. PMID 8550580.
- De Reuse H, Labigne A, Mengin-Lecreulx D (1997). "The Helicobacter pylori ureC gene codes for a phosphoglucosamine mutase". J. Bacteriol. 179 (11): 3488–93. doi: 10.1128/jb.179.11.3488-3493.1997. PMC 179139. PMID 9171391.
- Tomasz A; Wu, S; Van Heijenoort, J; De Lencastre, H; Mengin-Lecreulx, D; Tomasz, A (1997). "The femR315 gene from Staphylococcus aureus, the interruption of which results in reduced methicillin resistance, encodes a phosphoglucosamine mutase". J. Bacteriol. 179 (17): 5321–5. doi: 10.1128/jb.179.17.5321-5325.1997. PMC 179399. PMID 9286983.
- Mengin-Lecreulx D; Ferrari, P; Blanot, D; Van Heijenoort, J; Fassy, F; Mengin-Lecreulx, D (1999). "Reaction mechanism of phosphoglucosamine mutase from Escherichia coli". Eur. J. Biochem. 262 (1): 202–10. doi: 10.1046/j.1432-1327.1999.00373.x. PMID 10231382.
- Jolly L, Pompeo F, van Heijenoort J, Fassy F, Mengin-Lecreulx D (2000). "Autophosphorylation of phosphoglucosamine mutase from Escherichia coli". J. Bacteriol. 182 (5): 1280–5. doi: 10.1128/JB.182.5.1280-1285.2000. PMC 94413. PMID 10671448.
| Identifiers | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| EC no. | 5.4.2.10 | ||||||||
| 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 phosphoglucosamine mutase ( EC 5.4.2.10) is an enzyme that catalyzes the chemical reaction
- alpha-D-glucosamine 1-phosphate D-glucosamine 6-phosphate
Hence, this enzyme has one substrate, alpha-D-glucosamine 1-phosphate, and one product, D-glucosamine 6-phosphate.
This enzyme belongs to the family of isomerases, specifically the phosphotransferases ( α-D-phosphohexomutases), which transfer phosphate groups within a molecule. The systematic name of this enzyme class is alpha-D-glucosamine 1,6-phosphomutase. This enzyme participates in aminosugars metabolism.
Crystal structures of two bacterial phosphoglucosamine mutases are known (PDB entries 3I3W and 3PDK), from Francisella tularensis and Bacillus anthracis. Both share a similar dimeric quaternary structure, as well as conserved features of the active site, as found their enzyme superfamily, the α-D-phosphohexomutases.
References
- Mengin-Lecreulx D, van Heijenoort J (1996). "Characterization of the essential gene glmM encoding phosphoglucosamine mutase in Escherichia coli". J. Biol. Chem. 271 (1): 32–9. doi: 10.1074/jbc.271.1.32. PMID 8550580.
- De Reuse H, Labigne A, Mengin-Lecreulx D (1997). "The Helicobacter pylori ureC gene codes for a phosphoglucosamine mutase". J. Bacteriol. 179 (11): 3488–93. doi: 10.1128/jb.179.11.3488-3493.1997. PMC 179139. PMID 9171391.
- Tomasz A; Wu, S; Van Heijenoort, J; De Lencastre, H; Mengin-Lecreulx, D; Tomasz, A (1997). "The femR315 gene from Staphylococcus aureus, the interruption of which results in reduced methicillin resistance, encodes a phosphoglucosamine mutase". J. Bacteriol. 179 (17): 5321–5. doi: 10.1128/jb.179.17.5321-5325.1997. PMC 179399. PMID 9286983.
- Mengin-Lecreulx D; Ferrari, P; Blanot, D; Van Heijenoort, J; Fassy, F; Mengin-Lecreulx, D (1999). "Reaction mechanism of phosphoglucosamine mutase from Escherichia coli". Eur. J. Biochem. 262 (1): 202–10. doi: 10.1046/j.1432-1327.1999.00373.x. PMID 10231382.
- Jolly L, Pompeo F, van Heijenoort J, Fassy F, Mengin-Lecreulx D (2000). "Autophosphorylation of phosphoglucosamine mutase from Escherichia coli". J. Bacteriol. 182 (5): 1280–5. doi: 10.1128/JB.182.5.1280-1285.2000. PMC 94413. PMID 10671448.