D-serine dehydratase from Escherichia coli. DNA sequence and identification of catalytically inactive glycine to aspartic acid variants.

@article{Marceau1988DserineDF,
  title={D-serine dehydratase from Escherichia coli. DNA sequence and identification of catalytically inactive glycine to aspartic acid variants.},
  author={M Marceau and Elizabeth McFall and Sidney D Lewis and Jules A. Shafer},
  journal={The Journal of biological chemistry},
  year={1988},
  volume={263 32},
  pages={16926-33}
}
We have identified two glycyl residues whose integrity is essential for the catalytic competence of a model pyridoxal 5'-phosphate requiring enzyme, D-serine dehydratase from Escherichia coli. This was accomplished by isolating and sequencing the structural gene from wild type E. coli and from two mutant strains that produce inactive D-serine dehydratase. DNA sequencing indicated the presence of a single glycine to aspartic acid replacement in each variant. The amino acid replacements lie in a… CONTINUE READING

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