- Glyoxal Detoxification in Escherichia coli K-12 by NADPH Dependent Aldo-keto Reductases
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Changhan Lee , Insook Kim , Chankyu Park
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J. Microbiol. 2013;51(4):527-530. Published online August 30, 2013
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DOI: https://doi.org/10.1007/s12275-013-3087-8
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Glyoxal (GO) and methylglyoxal (MG) are reactive carbonyl compounds that are accumulated in vivo through various pathways. They are presumably detoxified through multiple pathways including glutathione (GSH)-dependent/independent glyoxalase systems and NAD(P)H dependent reductases. Previously, we reported an involvement of aldo-ketoreductases (AKRs) in MG detoxification. Here, we investigated the role of various AKRs (YqhE, YafB, YghZ, YeaE, and YajO) in GO metabolism. Enzyme activities of the AKRs to GO were measured, and GO sensitivities of the corresponding mutants were compared. In addition, we examined inductions of the AKR genes by GO. The results indicate that AKRs efficiently detoxify GO, among which YafB, YghZ, and YeaE are major players.
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Citations
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- Screening of Genes Related to Methylglyoxal Susceptibility
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Insook Kim , Joonho Kim , Bumchan Min , Changhan Lee , Chankyu Park
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J. Microbiol. 2007;45(4):339-343.
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DOI: https://doi.org/2563 [pii]
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Abstract
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Methylglyoxal (MG) is a reactive metabolite known to accumulate in certain physiological conditions. We attempted to isolate genes associated with this metabolite by genome-wide mutagenesis with TnphoA derivative. After screening on methylglyoxal-containing plate, we obtained insertions in three different genes, ydbD, yjjQ, and yqiI, which gave rise to reproducible MG-sensitive phenotypes in glyoxalase-deficient strain. In addition to its MG sensitivity, the insertion in yqiI exhibited an impaired motility resulting from a reduced flagellar expression.
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