Hartmann C, Klinman J P
Department of Chemistry, University of California, Berkeley 94720.
Biofactors. 1988 Jan;1(1):41-9.
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.
在过去十年中，吡咯喹啉醌已被证明是一系列细菌醇脱氢酶的一种新的氧化还原辅因子。最近的研究表明，这种辅因子也可能共价结合到真核铜胺氧化酶的活性位点上。在本综述中，我们提供了支持吡咯喹啉醌作为一种新型真核辅因子的证据。由于过去三年在机理研究方面取得的进展，以及对现有数据的重新审视，现在可以提出一个关于吡咯喹啉醌在酶催化胺氧化反应中作用的工作模型。
