• Corpus ID: 13509225

Location of three active site residues in the NH2-terminal sequence of the beta 2 subunit tryptophan synthase from Escherichia coli.

@article{Higgins1980LocationOT,
  title={Location of three active site residues in the NH2-terminal sequence of the beta 2 subunit tryptophan synthase from Escherichia coli.},
  author={William J. Higgins and Edith Wilson Miles and Thomas Fairwell},
  journal={The Journal of biological chemistry},
  year={1980},
  volume={255 2},
  pages={
          512-7
        }
}
The three known active site residues of the tryptophan synthase beta 2 subunit from Escherichia coli are shown to fall within 25 residues of each other in the primary sequence of the NH2-terminal region of the beta 2 subunit. These residues are: lysine-86, which forms a Schiff's base with pyridoxal phosphate; histidine-81 or histidine-85, which removes the alpha proton of L-serine; and cysteine-61, which reacts with bromoacetylpyridoxamine phosphate, an affinity label for the beta 2 subunit… 
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