PMID:10683264
| Citation |
Grant, GA, Xu, XL and Hu, Z (2000) Removal of the tryptophan 139 side chain in Escherichia coli D-3-phosphoglycerate dehydrogenase produces a dimeric enzyme without cooperative effects. Arch. Biochem. Biophys. 375:171-4 |
|---|---|
| Abstract |
Escherichia coli d-3-phosphoglycerate dehydrogenase (PGDH) is a homotetrameric enzyme whose activity is allosterically regulated by l-serine, the end-product of its metabolic pathway. Previous studies have shown that PGDH displays two modes of cooperative interaction. One is between the l-serine binding sites and the other is between the l-serine binding sites and the active sites. Tryptophan 139 participates in an intersubunit contact near the active site catalytic residues. Site-specific mutagenesis of tryptophan 139 to glycine results in the dissociation of the tetramer to a pair of dimers and in the loss of cooperativity in serine binding and between serine binding and inhibition. The results suggest that the magnitude of inhibition of activity at a particular active site is primarily dependent on serine binding to that subunit but that activity can be modulated in a cooperative manner by interaction with adjacent subunits. The disruption of the nucleotide domain interface in PGDH by mutating Trp-139 suggests the potential for a critical role of this interface in the cooperative allosteric processes in the native tetrameric enzyme. |
| Links |
PubMed Online version:10.1006/abbi.1999.1652 |
| Keywords |
Allosteric Regulation/drug effects; Allosteric Regulation/genetics; Binding Sites; Carbohydrate Dehydrogenases/antagonists & inhibitors; Carbohydrate Dehydrogenases/genetics; Carbohydrate Dehydrogenases/metabolism; Chromatography, Gel; Dimerization; Dose-Response Relationship, Drug; Enzyme Activation/drug effects; Enzyme Activation/genetics; Escherichia coli/enzymology; Mutagenesis, Site-Directed; Phosphoglycerate Dehydrogenase; Sequence Deletion/genetics; Serine/metabolism; Serine/pharmacology; Structure-Activity Relationship; Tryptophan/metabolism |
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