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J Biol Chem, Vol. 274, Issue 9, 5357-5361, February 26, 1999
From the Departments of Medicine & Molecular Biology and
Pharmacology, Washington University School of Medicine,
St. Louis, Missouri 63110
D-3-Phosphoglycerate
dehydrogenase (PGDH) from Escherichia coli is
allosterically inhibited by L-serine, the end product of its metabolic pathway. Previous results have shown that inhibition by
serine has a large effect on Vmax and only a
small or negligible effect on Km. PGDH is thus
classified as a V-type allosteric enzyme. In this study, the active
site of PGDH has been studied by site-directed mutagenesis to assess
the role of certain residues in substrate binding and catalysis. These
consist of a group of cationic residues (Arg-240, Arg-60, Arg-62,
Lys-39, and Lys-141') that potentially form an electrostatic
environment for the binding of the negatively charged substrate, as
well as the only tryptophan residue found in PGDH and which fits into a
hydrophobic pocket immediately adjacent to the active site histidine
residue. Interestingly, Trp-139' and Lys-141' are part of the
polypeptide chain of the subunit that is adjacent to the active site.
The results of mutating these residues show that Arg-240, Arg-60,
Arg-62, and Lys-141' play distinct roles in the binding of the
substrate to the active site. Mutants of Trp-139' show that this
residue may play a role in stabilizing the catalytic center of the
enzyme. Furthermore, these mutants appear to have a significant effect
on the cooperativity of serine inhibition and suggest a possible role
for Trp-139' in the cooperative interactions between subunits.
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