• Corpus ID: 24362978

Affinity labeling of the pyridoxal phosphate binding site of the beta2 subunit of Escherichia coli tryptophan synthase.

@article{Higgins1978AffinityLO,
  title={Affinity labeling of the pyridoxal phosphate binding site of the beta2 subunit of Escherichia coli tryptophan synthase.},
  author={W. Higgins and E. W. Miles},
  journal={The Journal of biological chemistry},
  year={1978},
  volume={253 13},
  pages={
          4648-52
        }
}
We have synthesized bromoacetylpyridoxamine phosphate and bromoacetylpyridoxamine and have shown that they meet three criteria for affinity labels of the beta2 subunit of tryptophan synthase: (i) the kinetic data of inactivation indicate that a binary complex is formed prior to covalent attachment; (ii) inactivation is largely prevented by the presence of pyridoxal phosphate; and (iii) inactivation is stoichiometric with incorporation of 0.7 to 0.8 mol of chromophore/mol of beta monomer. Our… 
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L-Methionine γ-Lyase: Its Essential Cysteine Residues
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References

hp://w w w .jb.org/ D ow nladed from 4652 New Affinity Labels for a Pyridoxal Phosphate Binding Site by gest on A uust 29
  • Rio&em. Biophys. Res. Commun
  • 1972