PMID:3053699
| Citation |
Marceau, M, McFall, E, Lewis, SD and Shafer, JA (1988) D-serine dehydratase from Escherichia coli. DNA sequence and identification of catalytically inactive glycine to aspartic acid variants. J. Biol. Chem. 263:16926-33 |
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| Abstract |
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 glycine-rich region of D-serine dehydratase well removed from pyridoxal 5'-phosphate-binding lysine 118 in the primary structure of the enzyme. The striking effect of these two glycine to aspartic acid replacements on catalytic activity, the conservation of the glycine-rich region in several pyridoxal 5'-phosphate-dependent enzymes that catalyze alpha/beta-eliminations, and the placement of similar glycine-rich sequences in well-characterized active site structures suggest that the glycine-rich region interacts with the cofactor at the active site of the enzyme. |
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| Keywords |
Amino Acid Sequence; Aspartic Acid/analysis; DNA, Bacterial/analysis; Escherichia coli/enzymology; Glycine/analysis; L-Serine Dehydratase/analysis; L-Serine Dehydratase/genetics; Molecular Sequence Data; Nucleotide Mapping; Protein Conformation |
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