Involvement of the conserved histidine-188 residue in the L-lactate dehydrogenase from Thermus caldophilus GK24 in allosteric regulation by fructose 1,6-bisphosphate
| Autor: | Gabriele Schroeder, Takahisa Ohta, Hiroshi Matsuzawa |
|---|---|
| Rok vydání: | 1988 |
| Předmět: |
Fructose 1
6-bisphosphate Phenylalanine Allosteric regulation Biophysics Fructose 1 6-bisphosphatase Dehydrogenase Biochemistry chemistry.chemical_compound Lactate dehydrogenase Pyruvic Acid Fructosediphosphates Histidine Thermus Site-directed mutagenesis Pyruvates Molecular Biology Binding Sites biology L-Lactate Dehydrogenase Fructose Cell Biology Hydrogen-Ion Concentration biology.organism_classification chemistry biology.protein Hexosediphosphates |
| Zdroj: | Biochemical and biophysical research communications. 152(3) |
| ISSN: | 0006-291X |
| Popis: | Summary The conserved histidine-188 residue of the L-lactate dehydrogenase of Thermus caldophilus GK 24, which is allosterically activated by fructose 1,6-bisphosphate, has been exchanged to phenylalanine by site-specific mutagenesis. In the mutant enzyme the strong stimulatory effect of fructose 1,6-bisphosphate is abolished. The analysis of the pH dependence of the activity indicates that the positive charge of the conserved His-188 residue is important for the interaction of the enzyme with the allosteric effector. |
| Databáze: | OpenAIRE |
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