Biochemistry: role of PQQ as a mammalian enzyme cofactor?

Nature. 2005 Feb 3;433(7025):E10; discussion E11-2. doi: 10.1038/nature03322.

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.

Publication types

  • Comment

MeSH terms

  • Alcohol Oxidoreductases / chemistry
  • Alcohol Oxidoreductases / metabolism
  • Aldehyde Oxidoreductases / chemistry
  • Aldehyde Oxidoreductases / metabolism
  • Amino Acid Motifs
  • Amino Acid Sequence
  • Animals
  • Coenzymes / metabolism*
  • Evolution, Molecular
  • L-Aminoadipate-Semialdehyde Dehydrogenase
  • Lysine / metabolism
  • Mice
  • Models, Molecular
  • PQQ Cofactor / metabolism*
  • Proteins / chemistry*
  • Proteins / metabolism*
  • Reproducibility of Results

Substances

  • Coenzymes
  • Proteins
  • U26 protein, mouse
  • PQQ Cofactor
  • Alcohol Oxidoreductases
  • alcohol dehydrogenase (acceptor)
  • Aldehyde Oxidoreductases
  • L-Aminoadipate-Semialdehyde Dehydrogenase
  • Lysine