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Role of PQQ as a mammalian enzyme cofactor?

Author

Listed:
  • Leigh M. Felton

    (School of Biological Sciences, University of Southampton)

  • Chris Anthony

    (School of Biological Sciences, University of Southampton)

Abstract

Arising from: T. Kasahara & T. Kato Nature 422, 832 (2003); see also communication from Rucker et al.; Kasahara et al. reply The announcement by Kasahara and Kato of a new redox-cofactor vitamin for mammals1, pyrroloquinoline quinone (PQQ), was based on their claim that an enzyme, predicted to be involved in mouse lysine metabolism, is a PQQ-dependent dehydrogenase. However, this claim was dependent on a sequence analysis using databases that inappropriately label β-propeller sequences as PQQ-binding motifs. What the evidence actually suggests is that the enzyme is an interesting novel protein that has a seven-bladed β-propeller structure, but there is nothing to indicate that it is a PQQ-dependent dehydrogenase.

Suggested Citation

  • Leigh M. Felton & Chris Anthony, 2005. "Role of PQQ as a mammalian enzyme cofactor?," Nature, Nature, vol. 433(7025), pages 10-10, February.
    • Handle: RePEc:nat:nature:v:433:y:2005:i:7025:d:10.1038_nature03322
    DOI: 10.1038/nature03322
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