title: A novel aldo-keto reductase from Escherichia coli can increase resistance to methylglyoxal toxicity.
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.
authors.affiliation: Department of Bioscience, University of Strathclyde, Royal College, 204 George Street, Glasgow G1 1XW, UK.
authors.forename: Anne W
authors.initials: AW
authors.lastname: Grant
authors.forename: Gavin
authors.initials: G
authors.lastname: Steel
authors.forename: Hugh
authors.initials: H
authors.lastname: Waugh
authors.forename: Elizabeth M
authors.initials: EM
authors.lastname: Ellis
mesh_terms: D000429:Alcohol Oxidoreductases / Q000235:genetics* / Q000378:metabolism*; D000449:Aldehyde Reductase; D000074408:Aldo-Keto Reductases; D003001:Cloning, Molecular; D004926:Escherichia coli / Q000187:drug effects / Q000201:enzymology* / Q000235:genetics*; D066298:In Vitro Techniques; D008969:Molecular Sequence Data; D016366:Open Reading Frames / Q000235:genetics; D011765:Pyruvaldehyde / Q000633:toxicity*; D017386:Sequence Homology, Amino Acid
chemical_list: D011765:Pyruvaldehyde; D000429:Alcohol Oxidoreductases; D000074408:Aldo-Keto Reductases; D000449:Aldehyde Reductase