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- W4214894808 abstract "A high-throughput assay for enzyme activity has been developed that is reaction independent. In this assay, a small-molecule yeast three-hybrid system is used to link enzyme catalysis to transcription of a reporter gene in vivo. Here we demonstrate the feasibility of this approach by using a well-studied enzyme-catalyzed reaction, cephalosporin hydrolysis by the Enterobacter cloacae P99 cephalosporinase (beta-lactam hydrolase, EC ). We show that the three-hybrid system can be used to read out cephalosporinase activity in vivo as a change in the level of transcription of a lacZ reporter gene and that the wild-type cephalosporinase can be isolated from a pool of inactive mutants by using a lacZ screen. The assay has been designed so that it can be applied to different chemical reactions without changing the components of the three-hybrid system. A reaction-independent high-throughput assay for protein function should be a powerful tool for protein engineering and enzymology, drug discovery, and proteomics. PMID: 12482929 Funding information This work was supported by: NIGMS NIH HHS, United States Grant ID: R01-GM62867 NIGMS NIH HHS, United States Grant ID: R01 GM062867" @default.
- W4214894808 created "2022-03-05" @default.
- W4214894808 creator A5075210236 @default.
- W4214894808 date "2003-01-07" @default.
- W4214894808 modified "2023-09-27" @default.
- W4214894808 title "Faculty Opinions recommendation of Chemical complementation: a reaction-independent genetic assay for enzyme catalysis." @default.
- W4214894808 doi "https://doi.org/10.3410/f.1011194.178262" @default.
- W4214894808 hasPublicationYear "2003" @default.
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