Biochemistry: role of PQQ as a mammalian enzyme cofactor?
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.
Felton
Leigh M
LM
School of Biological Sciences, University of Southampton, Southampton SO16 7PX, UK.
Anthony
Chris
C
D000429:Alcohol Oxidoreductases / Q000737:chemistry / Q000378:metabolism; D000445:Aldehyde Oxidoreductases / Q000737:chemistry / Q000378:metabolism; D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D000818:Animals; D003067:Coenzymes / Q000378:metabolism*; D019143:Evolution, Molecular; D050647:L-Aminoadipate-Semialdehyde Dehydrogenase; D008239:Lysine / Q000378:metabolism; D051379:Mice; D008958:Models, Molecular; D045542:PQQ Cofactor / Q000378:metabolism*; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism*; D015203:Reproducibility of Results
D003067:Coenzymes; D011506:Proteins; C473747:U26 protein, mouse; D045542:PQQ Cofactor; D000429:Alcohol Oxidoreductases; C019641:alcohol dehydrogenase (acceptor); D000445:Aldehyde Oxidoreductases; D050647:L-Aminoadipate-Semialdehyde Dehydrogenase; D008239:Lysine