pH-Dependent reversible inhibition of violaxanthin de-epoxidase by pepstatin related to protonation-induced structural change of the enzyme

Mitsuko Kawano, Tomohiko Kuwabara

Research output: Contribution to journalArticlepeer-review

9 Citations (Scopus)

Abstract

The redox enzyme violaxanthin de-epoxidase (VDE) was found to be sensitive to pepstatin, a specific inhibitor of aspartic protease. The inhibition was similar to that of aspartic protease in that it was reversible and accompanied by the protonation of the enzyme. Of the two peaks of VDE appearing on anion exchange chromatography, VDE-I predominated at pH 7.2. On lowering the pH of the chromatography, VDE-I decreased and VDE-II increased. Furthermore, re-chromatography of either peak yielded both peaks. These results suggest that VDE-I and VDE-II are interconvertible depending on pH, and thus, they represent the de-protonated and protonated forms of the enzyme, respectively. Presumably the protonation-induced structural change of the enzyme is responsible for the interaction with pepstatin, and also with substrate. (C) 2000 Federation of European Biochemical Societies.

Original languageEnglish
Pages (from-to)101-104
Number of pages4
JournalFEBS Letters
Volume481
Issue number2
DOIs
Publication statusPublished - 2000 Sep 15

Keywords

  • Pepstatin
  • Photoprotection
  • Protonation-induced conformational change
  • Violaxanthin de-epoxidase
  • Xanthophyll cycle

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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