PMID:12583903

Citation	Grant, AW, Steel, G, Waugh, H and Ellis, EM (2003) A novel aldo-keto reductase from Escherichia coli can increase resistance to methylglyoxal toxicity. FEMS Microbiol. Lett. 218:93-9
Abstract	A novel aldo-keto reductase (AKR) from Escherichia coli has been cloned, expressed and purified. This protein, YghZ, is distantly related (<40%) to mammalian aflatoxin dialdehyde reductases of the aldo-keto reductase AKR7 family and to potassium channel beta-subunits in the AKR6 family. The enzyme has been placed in a new AKR family (AKR14), with the designation AKR14A1. Sequences encoding putative homologues of this enzyme exist in many other bacteria. The enzyme can reduce several aldehyde and diketone substrates, including the toxic metabolite methylglyoxal. The K(m) for the model substrate 4-nitrobenzaldehyde is 1.06 mM and for the endogenous dicarbonyl methylglyoxal it is 3.4 mM. Overexpression of the recombinant enzyme in E. coli leads to increased resistance to methylglyoxal. It is possible that this enzyme plays a role in the metabolism of methylglyoxal, and can influence its levels in vivo.
Links	PubMed
Keywords	Alcohol Oxidoreductases/genetics; Alcohol Oxidoreductases/metabolism; Cloning, Molecular; Escherichia coli/drug effects; Escherichia coli/enzymology; Escherichia coli/genetics; Molecular Sequence Data; Open Reading Frames/genetics; Pyruvaldehyde/toxicity; Sequence Homology, Amino Acid
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