From famine to feast: the role of methylglyoxal production in Escherichia coli
| Autor: | Nuala A. Booth, B Dunbar, Ian R. Booth, Sabine Tötemeyer, W W Nichols |
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| Rok vydání: | 1998 |
| Předmět: |
Arabinose
Glycerol Mutant Carbon-Oxygen Lyases Molecular Sequence Data Methylglyoxal synthase Xylose Biology medicine.disease_cause Microbiology Phosphates chemistry.chemical_compound Open Reading Frames Xylose metabolism medicine Escherichia coli Molecular Biology chemistry.chemical_classification Methylglyoxal Gene Expression Regulation Bacterial Pyruvaldehyde Enzyme Glucose chemistry Biochemistry Genes Bacterial biology.protein Plasmids |
| Zdroj: | Molecular microbiology. 27(3) |
| ISSN: | 0950-382X |
| Popis: | The enzyme methylglyoxal synthase (MGS) was partially purified from Escherichia coli extracts, and the amino-terminal sequence of candidate proteins was determined, based on the native protein being a tetramer of about 69 kDa. Database analysis identified an open reading frame in the E. coli genome, YccG, corresponding to a protein of 16.9 kDa. When amplified and expressed from a controlled promoter, it yielded extracts that contained high levels of MGS activity. MGS expressed from the trc promoter accumulated to approximately 20% of total cell protein, representing approximately 900-fold enhanced expression. This caused no detriment during growth on glucose, and the level of methylglyoxal (MG) in the medium rose to only 0.08 mM. High-level expression of MGS severely compromised growth on xylose, arabinose and glycerol. A mutant lacking MGS was constructed, and it grew normally on a range of carbon sources and on low-phosphate medium. However, the mutant failed to produce MG during growth on xylose in the presence of cAMP, and growth was inhibited. |
| Databáze: | OpenAIRE |
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