Pyrroloquinoline quinone: a new redox cofactor in eukaryotic enzymes.
During the past decade pyrroloquinoline quinone has been shown to be a new redox cofactor for a range of bacterial alcohol dehydrogenases. Recent studies suggest that this cofactor may also be covalently bound to the active site of the eukaryotic copper amine oxidases. In this mini-review we present the evidence in support of pyrroloquinoline quinone as a novel eukaryotic cofactor. As a result of mechanistic advances during the last three years, together with a re-examination of previously existing data, a working model for the role of pyrroloquinoline quinone in enzyme-catalyzed amine oxidation reactions can be proposed.
Hartmann
C
C
Department of Chemistry, University of California, Berkeley 94720.
Klinman
J P
JP
D000818:Animals; D001665:Binding Sites; D003067:Coenzymes / Q000378:metabolism*; D010084:Oxidation-Reduction; D010088:Oxidoreductases / Q000378:metabolism*; D045542:PQQ Cofactor; D015363:Quinolones / Q000378:metabolism*
D003067:Coenzymes; D015363:Quinolones; D045542:PQQ Cofactor; D010088:Oxidoreductases