| Literature DB >> 16522074 |
Wenhui Zhou1, Michael P Valley, John Shultz, Erika M Hawkins, Laurent Bernad, Troy Good, Dave Good, Terry L Riss, Dieter H Klaubert, Keith V Wood.
Abstract
Novel bioluminogenic substrates were designed for probing monoamine oxidase (MAO) activity based on a simple and effective beta-elimination strategy. By modifying the amino group and the central core of luciferin derivatives, we have developed a series of substrates useful for assays of MAO A or B, or both. One of these substrates, exhibiting low Km values and high signal-to-background ratios with both isozymes, was shown to accurately measure the Ki values of known MAO inhibitors. This substrate is a key component in the development of a highly sensitive homogeneous MAO assay for high-throughput screening (HTS) of compounds in drug discovery and for monitoring MAO activity in complex biological systems. This design strategy should be applicable to fluorogenic MAO substrates and could broaden the structural requirements of substrates for other enzyme assays.Entities:
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Year: 2006 PMID： 16522074 DOI： 10.1021/ja058519o
Source DB: PubMed Journal: J Am Chem Soc ISSN： 0002-7863 Impact factor: 15.419