Escherichia coli phosphoenolpyruvate-dependent phosphotransferase system: mechanism of the phosphoryl-group transfer from phosphoenolpyruvate to HPr
| Autor: | George T. Robillard, Onno Misset |
|---|---|
| Přispěvatelé: | Groningen Biomolecular Sciences and Biotechnology, Enzymology |
| Rok vydání: | 1982 |
| Předmět: |
chemistry.chemical_classification
Chemistry Kinetics macromolecular substances PEP group translocation medicine.disease_cause Biochemistry In vitro Phosphoenolpyruvate carbohydrates (lipids) Enzyme Multienzyme Complexes Escherichia coli medicine bacteria Phosphorylation Binding site Phosphoenolpyruvate Sugar Phosphotransferase System Phosphoenolpyruvate carboxykinase Mathematics Protein Binding |
| Zdroj: | Biochemistry, 21(13), 3136-3142. AMER CHEMICAL SOC |
| ISSN: | 1520-4995 0006-2960 |
| DOI: | 10.1021/bi00256a016 |
| Popis: | The mechanism of phosphoryl-group transfer from phosphoenolpyruvate (PEP) to HPr, catalyzed by enzyme I of the Escherichia coli PEP-dependent phosphotransferase system, has been studied in vitro. Steady-state kinetics and isotope exchange measurements revealed that this reaction cannot be described by a classical ping-pong mechanism although phosphoenzyme I acts as an intermediate. The kinetic data indicate that HPr and PHPr occupy binding sites on enzyme I that do not overlap with the binding sites for PEP and pyruvate. As a result, binding interactions between HPr and enzyme I exist regardless of their phosphorylated state. A general mechanism is presented that describes the phosphorylation of HPr. The physiological implications of this mechanism are discussed. |
| Databáze: | OpenAIRE |
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