Lys296 and Arg299 residues in the C-terminus of MD-ACO1 are essential for a 1-aminocyclopropane-1-carboxylate oxidase enzyme activity

Ahrim Yoo, Young Sam Seo, Jin Won Jung, Soon Kee Sung, Woo Taek Kim, Weontae Lee, Dae Ryook Yang

Research output: Contribution to journalArticle

25 Citations (Scopus)

Abstract

The 1-aminocyclopropane-1-carboxylate (ACC) oxidase catalyzes the last step in the biosynthesis of ethylene from ACC in higher plants. The complex structure of ACC oxidase/Fe2+/H2O derived from Petunia hybrida has recently been established by X-ray crystallography and it provides a vast structural information for ACC oxidase. Our mutagenesis study shows that both Lys296 and Arg299 residues in the C-terminal helix play important roles in enzyme activity. Both K296R and R299K mutant proteins retain only 30-15% of their enzyme activities with respect to that of the wild-type, implying that the positive charges of C-terminal residues are involved in enzymatic reaction. Furthermore, the sequence alignment of ACC oxidases from 24 different species indicates an existence of the exclusively conserved motif (Lys296-Glu301) especially in the C-terminus. The structure model based on our findings suggests that the positive-charged surface in the C-terminal helix of the ACC oxidase could be a major stabilizer in the spatial arrangement of reactants and that the positive-charge network between the active site and C-terminus is critical for ACC oxidase activity.

Original languageEnglish
Pages (from-to)407-420
Number of pages14
JournalJournal of Structural Biology
Volume156
Issue number3
DOIs
Publication statusPublished - 2006 Dec 1

All Science Journal Classification (ASJC) codes

  • Structural Biology

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