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FAD-AMP lyase (cyclizing)

Part of the Springer Handbook of Enzymes book series (HDBKENZYMES, volume S7)

Keywords

Molecular Weight Bond Cleavage Reaction Type Dihydroxyacetone Kinase Monocyclic Compound 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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References

  1. [1]
    Fraiz, F.J.; Pinto, R.M.; Costas, M.J.; Avalos, M.; Canales, J.; Cabezas, A.; Cameselle, J.C.: Enzymic formation of riboflavin 4′,5′-cyclic phosphate from FAD: evidence for a specific low-Km FMN cyclase in rat liver. Biochem. J., 330, 881–888 (1998)PubMedGoogle Scholar
  2. [2]
    Cabezas, A.; Pinto, R.M.; Fraiz, F.; Canales, J.; Gonzalez-Santiago, S.; Cameselle, J.C.: Purification, characterization, and substrate and inhibitor structure-activity studies of rat liver FAD-AMP lyase (cyclizing): Preference for FAD and specificity for splitting ribonucleoside diphosphate-X into ribonucleotide and a five-atom cyclic phosphodiester of X, either a monocyclic compound or a cis-bicyclic phosphodiester-pyranose fusion. Biochemistry, 40, 13710–13722 (2001)CrossRefPubMedGoogle Scholar
  3. [3]
    Cabezas, A.; Costas, M.J.; Pinto, R.M.; Couto, A.; Cameselle, J.C.: Identification of human and rat FAD-AMP lyase (cyclic FMN forming) as ATP-dependent dihydroxyacetone kinases. Biochem. Biophys. Res. Commun., 338, 1682–1689 (2005)CrossRefPubMedGoogle Scholar

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