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- W2031146914 abstract "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." @default.
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- W2031146914 date "1998-02-01" @default.
- W2031146914 modified "2023-10-15" @default.
- W2031146914 title "From famine to feast: the role of methylglyoxal production in <i>Escherichia coli</i>" @default.
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- W2031146914 doi "https://doi.org/10.1046/j.1365-2958.1998.00700.x" @default.
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