Characterization of Arabidopsis secretory phospholipase A 2-γ cDNA and its enzymatic properties

Sung Chul Bahn, Hyoung Yool Lee, Hae Jin Kim, Stephen B. Ryu, Jeong Sheop Shin

Research output: Contribution to journalArticlepeer-review

30 Citations (Scopus)


Plant secretory phospholipases A2 (sPLA2s) probably play important roles in phospholipid signaling based on the data reported from other organisms, but their functions are poorly understood because of the lack of cloned sPLA2 genes. In this study, we cloned and characterized an Arabidopsis secretory phospholipase A2-γ (AtsPLA 2-γ) cDNA, and examined its enzymatic properties. The recombinant protein of AtsPLA2-γ showed maximal enzyme activity at pH 8.0, and required Ca2+ for activity. Moreover, AtsPLA2-γ showed sn-2 position specificity but no prominent acyl preference, though it showed head group specificity to phosphatidylethanolamine rather than to phosphatidylcholine. AtsPLA 2-γ was found to predominate in the mature flower rather than in other tissues, and subcellular localization analysis confirmed that AtsPLA2-γ is secreted into the intercellular space.

Original languageEnglish
Pages (from-to)113-118
Number of pages6
JournalFEBS Letters
Issue number1-2
Publication statusPublished - 2003 Oct 9


  • AtsPLA-γ
  • Lysophospholipid
  • Phosphatidylcholine
  • Phosphatidylethanolamine
  • Phospholipid
  • Secretory phospholipase A

ASJC Scopus subject areas

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


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