Functional Analysis of the AKR4C Subfamily of Arabidopsis thaliana : Model Structures, Substrate Specificity, Acrolein Toxicity, and Responses to Light and [CO₂]

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  • SAITO Ryota
    Department of Biological and Environmental Science, Faculty of Agriculture, Graduate School of Agricultural Science, Kobe University
  • SHIMAKAWA Ginga
    Department of Biological and Environmental Science, Faculty of Agriculture, Graduate School of Agricultural Science, Kobe University
  • NISHI Akiko
    Department of Biological and Environmental Science, Faculty of Agriculture, Graduate School of Agricultural Science, Kobe University
  • IWAMOTO Tatsuya
    Department of Biological and Environmental Science, Faculty of Agriculture, Graduate School of Agricultural Science, Kobe University
  • SAKAMOTO Katsuhiko
    Department of Biological and Environmental Science, Faculty of Agriculture, Graduate School of Agricultural Science, Kobe University
  • YAMAMOTO Hiroshi
    Faculty of Nutrition, Kobe Gakuin University
  • AMAKO Katsumi
    Department of Botany, Graduate School of Science, Kyoto University
  • MAKINO Amane
    Department of Agriculture, Graduate School of Agricultural Science, Tohoku University CREST, JST
  • MIYAKE Chikahiro
    Department of Biological and Environmental Science, Faculty of Agriculture, Graduate School of Agricultural Science, Kobe University CREST, JST

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  • Functional Analysis of the AKR4C Subfamily of <i>Arabidopsis thaliana</i>: Model Structures, Substrate Specificity, Acrolein Toxicity, and Responses to Light and [CO<sub>2</sub>]

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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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