Methylglyoxal inhibition of cytosolic ascorbate peroxidase from Nicotiana tabacum

Md Anamul Hoque, Misugi Uraji, Akiko Torii, Mst Nasrin Akhter Banu, Izumi C. Mori, Yoshimasa Nakamura, Yoshiyuki Murata

Research output: Contribution to journalArticlepeer-review

36 Citations (Scopus)


Methylglyoxal (MG) is one of the aldehydes accumulated in plants under environmental stress. Cytosolic ascorbate peroxidase (cAPX) plays a key role in the protection of cells from oxidative damage by scavenging reactive oxygen species in higher plants. A cDNA encoding cAPX, named NtcAPX, was isolated from Nicotiana tabacum. We characterized recombinant NtcAPX (rNtcAPX) as a fusion protein with glutathione S-transferase to investigate the effects of MG on APX. NtcAPX consists of 250 amino acids and has a deduced molecular mass of 27.5 kDa. The rNtcAPX showed a higher APX activity. MG treatments resulted in a reduction of APX activity and modifications of amino groups in rNtcAPX with increasing Km for ascorbate. On the contrary, neither NaCl nor cadmium reduced the activity of APX. The present study suggests that inhibition of APX is in part due to the modification of amino acids by MG.

Original languageEnglish
Pages (from-to)315-321
Number of pages7
JournalJournal of Biochemical and Molecular Toxicology
Issue number8
Publication statusPublished - Aug 1 2012


  • Cytosolic Ascorbate Peroxidase
  • HO
  • Methylglyoxal
  • Salt Stress

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Medicine
  • Molecular Biology
  • Toxicology
  • Health, Toxicology and Mutagenesis


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