Substitution of aspartate and glutamate for active center histidines in the Escherichia coli phosphoenolpyruvate:sugar phosphotransferase system maintain phosphotransfer potential
| Autor: | Jason Kindrachuk, Scott Napper, Stephen J. Brokx, E. Bruce Waygood, Elliott Pally, Louis T. J. Delbaere |
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| Rok vydání: | 2001 |
| Předmět: |
inorganic chemicals
Glutamic Acid macromolecular substances Biochemistry Active center Serine Structure-Activity Relationship Bacterial Proteins Escherichia coli Histidine Threonine Phosphorylation Phosphoenolpyruvate Sugar Phosphotransferase System Molecular Biology chemistry.chemical_classification Aspartic Acid Chemistry Cell Biology PEP group translocation Amino acid enzymes and coenzymes (carbohydrates) bacteria lipids (amino acids peptides and proteins) Phosphoenolpyruvate carboxykinase Cysteine |
| Zdroj: | The Journal of biological chemistry. 276(45) |
| ISSN: | 0021-9258 |
| Popis: | The active center histidines of the Escherichia coli phosphoenolpyruvate:sugar phosphotransferase system proteins; histidine-containing protein, enzyme I, and enzyme IIA(Glc) were substituted with a series of amino acids (serine, threonine, tyrosine, cysteine, aspartate, and glutamate) with the potential to undergo phosphorylation. The mutants [H189E]enzyme I, [H15D]HPr, and [H90E]enzyme IIA(Glc) retained ability for phosphorylation as indicated by [(32)P]phosphoenolpyruvate labeling. As the active center histidines of both enzyme I and enzyme IIA(Glc) undergo phosphorylation of the N(epsilon2) atom, while HPr is phosphorylated at the N(delta1) atom, a pattern of successful substitution of glutamates for N(epsilon2) phosphorylations and aspartates for N(delta1) phosphorylations emerges. Furthermore, phosphotransfer between acyl residues: P-aspartyl to glutamyl and P-glutamyl to aspartyl was demonstrated with these mutant proteins and enzymes. |
| Databáze: | OpenAIRE |
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