| adenosylcobalamin/α-ribazole phosphatase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.1.3.73 | ||||||||
| CAS no. | 251991-06-7 | ||||||||
| 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 | ||||||||
| |||||||||
The primary biochemical reaction catalyzed by the enzyme adenosylcobalamin/α-ribazole phosphatase (formerly α-ribazole phosphatase) [1] (EC 3.1.3.73) is
- adenosylcobalamin 5′-phosphate + H2O = coenzyme B12 + phosphate
This enzyme can also catalyze the following reaction in vitro, however it is not the biologically relevant reaction
- α-ribazole 5′-phosphate + H2O α-ribazole + phosphate
This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name is adenosylcobalamin/α-ribazole-5′-phosphate phosphohydrolase. This enzyme is also called CobC. It is part of the biosynthetic pathway to cobalamin (vitamin B12) in bacteria. [2] [3]
As of late 2007, 16 structures have been solved for this class of enzymes, with PDB accession codes 2ENU, 2ENW, 2EOA, 2OWE, 2P2Y, 2P2Z, 2P30, 2P6M, 2P6O, 2P75, 2P77, 2P78, 2P79, 2P9Y, 2P9Z, and 2PA0.
- ^ O'Toole GA, Trzebiatowski JR, Escalante-Semerena JC (1994). "The cobC gene of Salmonella typhimurium codes for a novel phosphatase involved in the assembly of the nucleotide loop of cobalamin". J. Biol. Chem. 269 (42): 26503–11. PMID 7929373.
- ^ Warren MJ, Raux E, Schubert HL, Escalante-Semerena JC (2002). "The biosynthesis of adenosylcobalamin (vitamin B12)". Nat. Prod. Rep. 19 (4): 390–412. doi: 10.1039/b108967f. PMID 12195810.
- ^ Zayas CL, Escalante-Semerena JC (2007). "Reassessment of the late steps of coenzyme B12 synthesis in Salmonella enterica: evidence that dephosphorylation of adenosylcobalamin-5′-phosphate by the CobC phosphatase is the last step of the pathway". J. Bacteriol. 189 (6): 2210–8. doi: 10.1128/jb.01665-06. PMC 1899380. PMID 17209023.
| adenosylcobalamin/α-ribazole phosphatase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.1.3.73 | ||||||||
| CAS no. | 251991-06-7 | ||||||||
| 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 | ||||||||
| |||||||||
The primary biochemical reaction catalyzed by the enzyme adenosylcobalamin/α-ribazole phosphatase (formerly α-ribazole phosphatase) [1] (EC 3.1.3.73) is
- adenosylcobalamin 5′-phosphate + H2O = coenzyme B12 + phosphate
This enzyme can also catalyze the following reaction in vitro, however it is not the biologically relevant reaction
- α-ribazole 5′-phosphate + H2O α-ribazole + phosphate
This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name is adenosylcobalamin/α-ribazole-5′-phosphate phosphohydrolase. This enzyme is also called CobC. It is part of the biosynthetic pathway to cobalamin (vitamin B12) in bacteria. [2] [3]
As of late 2007, 16 structures have been solved for this class of enzymes, with PDB accession codes 2ENU, 2ENW, 2EOA, 2OWE, 2P2Y, 2P2Z, 2P30, 2P6M, 2P6O, 2P75, 2P77, 2P78, 2P79, 2P9Y, 2P9Z, and 2PA0.
- ^ O'Toole GA, Trzebiatowski JR, Escalante-Semerena JC (1994). "The cobC gene of Salmonella typhimurium codes for a novel phosphatase involved in the assembly of the nucleotide loop of cobalamin". J. Biol. Chem. 269 (42): 26503–11. PMID 7929373.
- ^ Warren MJ, Raux E, Schubert HL, Escalante-Semerena JC (2002). "The biosynthesis of adenosylcobalamin (vitamin B12)". Nat. Prod. Rep. 19 (4): 390–412. doi: 10.1039/b108967f. PMID 12195810.
- ^ Zayas CL, Escalante-Semerena JC (2007). "Reassessment of the late steps of coenzyme B12 synthesis in Salmonella enterica: evidence that dephosphorylation of adenosylcobalamin-5′-phosphate by the CobC phosphatase is the last step of the pathway". J. Bacteriol. 189 (6): 2210–8. doi: 10.1128/jb.01665-06. PMC 1899380. PMID 17209023.