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- W2485673883 abstract "Prephenate dehydratase of Corynebacterium glutamicum catalyzes the biosynthesis of phenylalanine from chorismate, which is the common precursor of many aromatic compounds, including the amino acids tyrosine, trytophan and phenylalanine. Phenylalanine biosynthesis is regulated predominantly through phenylalanine-mediated inhibition of pheA transcription and by feedback inhibition on the enzymatic activities of prephenate dehydratase and chorismate mutase. To better understand the catalytic mechanism of prephenate dehydratase and the structural basis of feedback inhibition, we would like to determine the structure of this enzyme by X-ray crystallography. It has been shown by Derewenda that targeted mutagenesis of surface patches containing residues with large flexible side chains and their replacement with smaller amino acids lead to effective preparation of X-ray quality crystals of proteins. We adopted the same approach by introducing mutations on the predicted surface regions of prephenate dehydratase, including PD35 (E35A/E37A/ Q38A), PD179 (R179A/R182A), PD236 (R236A/R239A/K240A) and PD284 (R284A/E286A /D287A). From the crystals of PD284 (R284A/E286A /D287A) protein, we obtained diffraction patterns of about 5.6 A resolution, but the crystal quality remains to be improved. In the future, we will use PD284 as template to introduce more surface mutations to further enhance crystal quality." @default.
- W2485673883 created "2016-08-23" @default.
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- W2485673883 date "2007-01-01" @default.
- W2485673883 modified "2023-09-23" @default.
- W2485673883 title "以循理式蛋白表面胺基酸突變改善 Prephenate dehydratase 結晶的繞射品質" @default.
- W2485673883 hasPublicationYear "2007" @default.
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