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- W2022758487 abstract "We present an improved and simple direct assay for formation of inorganic sulfide from l-cysteine in a β-replacement reaction catalyzed by tryptophan synthase. This method provides a useful enzymatic assay for pyridoxal phosphate-dependent β-replacement reactions in which the amino acid substrate is l-cysteine and the cosubstrate is 2-mercaptoethanol. The assay should be applicable to similar reactions with l-cysteine and other cosubstrates. The method has several advantages over other methods which have been used to assay similar β-replacement reactions. The assay is highly reproducible and sensitive and is conveniently carried out in disposable 1.5-ml centrifuge tubes. The color remains stable for several hours. The thiol compounds l-cysteine and 2-mercaptoethanol do not interfere at the concentrations used. The method has useful applications to studies of the rates and reaction specificities of several other pyridoxal phosphate enzymes which catalyze β-replacement reactions. We demonstrate the use of the method to study the effects of site-directed mutagenesis on the reaction specificity and mechanism of the tryptophan synthase α2β2 complex." @default.
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- W2022758487 date "1991-03-01" @default.
- W2022758487 modified "2023-10-17" @default.
- W2022758487 title "A colorimetric assay for a pyridoxal phosphate-dependent β-replacement reaction with l-cysteine: Application to studies of wild-type and mutant tryptophan synthase α2β2 complexes" @default.
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- W2022758487 doi "https://doi.org/10.1016/0003-2697(91)90009-i" @default.
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