Identification of a phosphoenolpyruvate:fructose phosphotransferase system (fructose-1-phosphate forming) in Listeria monocytogenes
| Autor: | Milton H. Saier, Jonathan Reizer, W J Mitchell, C Hoischen, Christopher D. Herring |
|---|---|
| Rok vydání: | 1993 |
| Předmět: |
Fructose
macromolecular substances Microbiology Fructokinase Fructokinases chemistry.chemical_compound Bacterial Proteins Phosphoenolpyruvate—protein phosphotransferase Phosphorylation Enzyme inducer Phosphoenolpyruvate Sugar Phosphotransferase System Molecular Biology biology Fructosephosphates Phosphotransferases (Nitrogenous Group Acceptor) PEP group translocation Listeria monocytogenes Fructose 1-phosphate carbohydrates (lipids) chemistry Biochemistry Enzyme Induction biology.protein bacteria Phosphoenolpyruvate carboxykinase Research Article |
| Zdroj: | Journal of Bacteriology. 175:2758-2761 |
| ISSN: | 1098-5530 0021-9193 |
| DOI: | 10.1128/jb.175.9.2758-2761.1993 |
| Popis: | Listeria monocytogenes is a gram-positive bacterium whose carbohydrate metabolic pathways are poorly understood. We provide evidence for an inducible phosphoenolpyruvate (PEP):fructose phosphotransferase system (PTS) in this pathogen. The system consists of enzyme I, HPr, and a fructose-specific enzyme II complex which generates fructose-1-phosphate as the cytoplasmic product of the PTS-catalyzed vectorial phosphorylation reaction. Fructose-1-phosphate kinase then converts the product of the PTS reaction to fructose-1,6-bisphosphate. HPr was shown to be phosphorylated by [32P]PEP and enzyme I as well as by [32P]ATP and a fructose-1,6-bisphosphate-activated HPr kinase like those found in other gram-positive bacteria. Enzyme I, HPr, and the enzyme II complex of the Listeria PTS exhibit enzymatic cross-reactivity with PTS enzyme constituents from Bacillus subtilis and Staphylococcus aureus. |
| Databáze: | OpenAIRE |
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