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- W293870047 abstract "Two of the 5 sulfhydryl residues of the β2 subunit of tryptophan synthase have previously been shown to react with N-ethylmaleimide and to have active site roles. We now show that the single sulfhydryl which reacts with N-ethylmaleimide in the presence of pyridoxal phosphate is cysteine-170. The essential sulfhydryl which reacts with N-ethylmaleimide or with 2-nitro-5-thiocyanobenzoic acid after removal of pyridoxal phosphate is cysteine-230. The affinity reagent, bromoacetylpyridoxamine phosphate, reacts variably with cysteine-62 or with cysteine-230." @default.
- W293870047 created "2016-06-24" @default.
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- W293870047 date "1980-04-01" @default.
- W293870047 modified "2023-09-23" @default.
- W293870047 title "Location of the reactive sulfhydryl residues in the primary sequence of the β2 subunit of tryptophan synthase of Escherichiacoli" @default.
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- W293870047 doi "https://doi.org/10.1016/0006-291x(80)90610-5" @default.
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