Bioscience, Biotechnology, and Biochemistry
Online ISSN : 1347-6947
Print ISSN : 0916-8451
Environmental Science Regular Papers
Functional Analysis of the AKR4C Subfamily of Arabidopsis thaliana: Model Structures, Substrate Specificity, Acrolein Toxicity, and Responses to Light and [CO2]
Ryota SAITOGinga SHIMAKAWAAkiko NISHITatsuya IWAMOTOKatsuhiko SAKAMOTOHiroshi YAMAMOTOKatsumi AMAKOAmane MAKINOChikahiro MIYAKE
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Supplementary material

2013 Volume 77 Issue 10 Pages 2038-2045

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Abstract

In Arabidopsis thaliana, the aldo-keto reductase (AKR) family includes four enzymes (The AKR4C subfamily: AKR4C8, AKR4C9, AKR4C10, and AKR4C11). AKR4C8 and AKR4C9 might detoxify sugar-derived reactive carbonyls (RCs). We analyzed AKR4C10 and AKR4C11, and compared the enzymatic functions of the four enzymes. Modeling of protein structures based on the known structure of AKR4C9 found an (α/β)8-barrel motif in all four enzymes. Loop structures (A, B, and C) which determine substrate specificity, differed among the four. Both AKR4C10 and AKR4C11 reduced methylglyoxal. AKR4C10 reduced triose phosphates, dihydroxyacetone phosphate (DHAP), and glyceraldehydes 3-phosphate (GAP), the most efficiently of all the AKR4Cs. Acrolein, a lipid-derived RC, inactivated the four enzymes to different degrees. Expression of the AKR4C genes was induced under high-[CO2] and high light, when photosynthesis was enhanced and photosynthates accumulated in the cells. These results suggest that the AKR4C subfamily contributes to the detoxification of sugar-derived RCs in plants.

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© 2013 by Japan Society for Bioscience, Biotechnology, and Agrochemistry
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