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- W2076756868 abstract "Tryptophan 248, located in the active site of tryptophanase from Escherichia coli, has been replaced with phenylalanine by site-directed mutagenesis. Judging from CD and fluorescence spectra, the global structure of the mutant enzyme was found to be the same as that of the wild-type enzyme. The binding affinity of the mutant enzyme for the coenzyme pyridoxal 5′-phosphate (PLP) was reduced tenfold compared to the wild-type enzyme. Kinetic analyses under PLP-saturated conditions indicated that the Km values of the mutant enzyme for substrates are the same as those of wild-type enzyme but the kcat values are decreased to about 85%, which accounts for the overall activity decrease. These findings suggest that tryptophan 248 interacts closely with PLP and plays an important role in the catalytic reaction." @default.
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- W2076756868 date "1990-12-01" @default.
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- W2076756868 title "Role of tryptophan 248 in the active site of tryptophanase from Escherichia coli" @default.
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- W2076756868 doi "https://doi.org/10.1016/s0006-291x(05)80100-7" @default.
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