EC 3.6.1.53 - Mn2+-dependent ADP-ribose/CDP-alcohol diphosphatase

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IntEnz Enzyme Nomenclature
EC 3.6.1.53

Names

Accepted name:
Mn2+-dependent ADP-ribose/CDP-alcohol diphosphatase
Other names:
Mn2+-dependent ADP-ribose/CDP-alcohol pyrophosphatase
ADPRibase-Mn
Systematic name:
CDP-choline phosphohydrolase

Reactions

Cofactor

Comments:

Requires Mn2+, which cannot be replaced by Mg2+, for activity. ADP-D-ribose, CDP-choline, CDP-ethanolamine and ADP are substrates for this enzyme but ADP-D-glucose, UDP-D-glucose, CDP-D-glucose, CDP, CMP and AMP are not hydrolysed [2]. In rat, the enzyme is found predominantly in thymus and spleen.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
UniProtKB/Swiss-Prot:

References

  1. Canales, J., Pinto, R.M., Costas, M.J., Hernández, M.T., Miró, A., Bernet, D., Fernández, A. and Cameselle, J.C.
    Rat liver nucleoside diphosphosugar or diphosphoalcohol pyrophosphatases different from nucleotide pyrophosphatase or phosphodiesterase I: substrate specificities of Mg2+-and/or Mn2+-dependent hydrolases acting on ADP-ribose.
    Biochim. Biophys. Acta 1246: 167-177 (1995). [PMID: 7819284]
  2. Canales, J., Fernández, A., Ribeiro, J.M., Cabezas, A., Rodrigues, J.R., Cameselle, J.C. and Costas, M.J.
    Mn2+-dependent ADP-ribose/CDP-alcohol pyrophosphatase: a novel metallophosphoesterase family preferentially expressed in rodent immune cells.
    Biochem. J. 413: 103-113 (2008). [PMID: 18352857]

[EC 3.6.1.53 created 2008]