| Literature DB >> 2855582 |
Abstract
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.Entities:
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Year: 1988 PMID: 2855582
Source DB: PubMed Journal: Biofactors ISSN: 0951-6433 Impact factor: 6.113