Abstract
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.
MeSH terms
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Alcohol Oxidoreductases / chemistry
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Alcohol Oxidoreductases / metabolism
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Aldehyde Oxidoreductases / chemistry
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Aldehyde Oxidoreductases / metabolism
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Amino Acid Motifs
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Amino Acid Sequence
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Animals
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Coenzymes / metabolism*
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Evolution, Molecular
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L-Aminoadipate-Semialdehyde Dehydrogenase
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Lysine / metabolism
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Mice
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Models, Molecular
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PQQ Cofactor / metabolism*
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Proteins / chemistry*
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Proteins / metabolism*
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Reproducibility of Results
Substances
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Coenzymes
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Proteins
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U26 protein, mouse
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PQQ Cofactor
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Alcohol Oxidoreductases
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alcohol dehydrogenase (acceptor)
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Aldehyde Oxidoreductases
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L-Aminoadipate-Semialdehyde Dehydrogenase
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Lysine