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• W2043280156 abstract "We cloned and sequenced the tryptophanase structural gene of Escherichia coli B/1t7-A strain. The results indicate that tryptophanase proteins of E. coli B/1t7-A and K-12 are identical. When cysteine residues in tryptophanase were chemically modified with 5,5'-dithiobis (2-nitrobenzoic acid) (DTNB), the stabilizing effect of the active cations such as K+ and NH4+ was abolished. In consideration of our previous results that Cys-298 was selectively modified by SH reagents [Honda T. et al. (1986) J. Chromatogr. 371, 353-360], Cys-298 seems to have a close relation to the expression of the effect of monovalent cations. Fluorescence decay measurement of the holoenzyme revealed that the fluorescence lifetime derived from the coenzyme, pyridoxal 5'-phosphate (PLP), was dependent on coexisting monovalent cations, whereas that of the tryptophyl residue was not, in either the apo- or the holoenzyme preparation. The results of the synchrotron small-angle X-ray scattering measurements showed that radii of gyration which reflect the size and shape of the enzyme were constant at around 38 A irrespective of the presence or absence of the K+ ion. These results suggest that the monovalent cations interact specifically with the PLP-binding site, and that the conformational change of enzyme protein caused by the monovalent-cation binding is limited to a small range. The above results are compatible with the possibility that Cys-298 is involved in the formation of monovalent cation binding site in the holoenzyme." @default.
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• W2043280156 date "1989-06-01" @default.
• W2043280156 modified "2023-09-25" @default.
• W2043280156 title "Role of cysteine residues in tryptophanase for monovalent cation-induced activation" @default.
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• W2043280156 doi "https://doi.org/10.1016/0300-9084(89)90087-4" @default.
• W2043280156 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/2502187" @default.
• W2043280156 hasPublicationYear "1989" @default.
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