4.4 Article

Glyoxal Detoxification in Escherichia coli K-12 by NADPH Dependent Aldo-keto Reductases

Journal

JOURNAL OF MICROBIOLOGY
Volume 51, Issue 4, Pages 527-530

Publisher

MICROBIOLOGICAL SOCIETY KOREA
DOI: 10.1007/s12275-013-3087-8

Keywords

glyoxal; methylglyoxal; aldo-keto reductase

Categories

Funding

  1. Korea Institute of Planning and Evaluation for Technology in food, agriculture, forestry, and fisheries [110056032HD120]
  2. National Research Foundation of Korea [N01120620]
  3. National Research Foundation of Korea [2012R1A1A2041712] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)

Ask authors/readers for more resources

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.

Authors

I am an author on this paper
Click your name to claim this paper and add it to your profile.

Reviews

Primary Rating

4.4
Not enough ratings

Secondary Ratings

Novelty
-
Significance
-
Scientific rigor
-
Rate this paper

Recommended

No Data Available
No Data Available