
The announcement by Kasahara and Kato of a new redox-cofactor vitamin for mammals, 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 beta-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 beta-propeller structure, but there is nothing to indicate that it is a PQQ-dependent dehydrogenase.
Models, Molecular, Lysine, Amino Acid Motifs, Coenzymes, PQQ Cofactor, Proteins, Reproducibility of Results, Aldehyde Oxidoreductases, Evolution, Molecular, Alcohol Oxidoreductases, L-Aminoadipate-Semialdehyde Dehydrogenase, Mice, Animals, Amino Acid Sequence
Models, Molecular, Lysine, Amino Acid Motifs, Coenzymes, PQQ Cofactor, Proteins, Reproducibility of Results, Aldehyde Oxidoreductases, Evolution, Molecular, Alcohol Oxidoreductases, L-Aminoadipate-Semialdehyde Dehydrogenase, Mice, Animals, Amino Acid Sequence
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