Role of PQQ as a mammalian enzyme cofactor?

Leigh M. Felton and Chris Anthony ()
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Leigh M. Felton: School of Biological Sciences, University of Southampton
Chris Anthony: School of Biological Sciences, University of Southampton

Nature, 2005, vol. 433, issue 7025, E10-E10

Abstract: 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.

Date: 2005
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DOI: 10.1038/nature03322

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