Alpha-ribazole phosphatase

adenosylcobalamin-5'-phosphate (AdoCbl-5'-P) phosphatase
Identifiers
EC number 3.1.3.73
CAS number 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 adenosylcobalamin-5'-phosphate phosphatase(formerly: alpha-ribazole phosphatase) (EC 3.1.3.73) enzyme is

AdoCbl-5'-P + H2O AdoCbl + phosphate

This enzyme can also catalyze the following reaction in vitro, however it is not the biologically relevant reaction

alpha-ribazole 5'-phosphate + H2O alpha-ribazole + phosphate

Thus, the two substrates of this enzyme are adenosylcobalamin-5'-phosphate and H2O, whereas its two products are adenosylcobalamin and phosphate.

This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name of this enzyme class is adenosylcobalamin-5'-phosphate phosphohydrolase. This enzyme is also called CobC. This enzyme participates in adenosylcobalamin (coenzyme B12) biosynthesis.

Structural studies

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.

References

    • 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.


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