Functional analysis of the AKR4C subfamily of arabidopsis thaliana: Model structures, substrate specificity, acrolein toxicity, and responses to light and [CO2]

Ryota Saito, Ginga Shimakawa, Akiko Nishi, Tatsuya Iwamoto, Katsuhiko Sakamoto, Hiroshi Yamamoto, Katsumi Amako, Amane Makino, Chikahiro Miyake

Research output: Contribution to journalArticlepeer-review

26 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)2038-2045
Number of pages8
JournalBioscience, Biotechnology and Biochemistry
Volume77
Issue number10
DOIs
Publication statusPublished - 2013

Keywords

  • Aldo-keto reductase (AKR)
  • Methylglyoxal (MG)
  • Plant diabetes
  • Reactive carbonyls (RCs)
  • Triose phosphate (TP)

ASJC Scopus subject areas

  • Biotechnology
  • Analytical Chemistry
  • Biochemistry
  • Applied Microbiology and Biotechnology
  • Molecular Biology
  • Organic Chemistry

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