Acta Physiologiae Plantarum

, 41:151 | Cite as

Advances in plant GDSL lipases: from sequences to functional mechanisms

  • Li-Na Ding
  • Ming Li
  • Wei-Jie Wang
  • Jun Cao
  • Zheng Wang
  • Ke-Ming Zhu
  • Yan-Hua Yang
  • Yu-Long Li
  • Xiao-Li TanEmail author


GDSL lipases form multigene families in Arabidopsis, rice and some other sequenced plant species. Unlike classical GxSxG motif-containing lipases, this new sub-family of lipolytic enzymes possesses a GDSL sequence motif (GDSxxDxG), and members are active in the hydrolysis and synthesis of a variety of lipids. Research on plant GDSL lipases started later than studies of microbial and animal GDSL lipases; therefore, our knowledge regarding plant GDSL lipases, from sequences to functional mechanisms, is limited. Recently, some GDSL lipase genes have been cloned and identified in different plant species. In this paper, we present a comprehensive review of the advances in research on plant GDSL lipases, which include their structures, distributions, biochemical activities, expression patterns and biological functions. Plant GDSL lipases have very flexible enzyme active sites, which can lead to extensive substrate binding and result in multifunctional properties. They play important roles in many physiological and biochemical processes, such as plant growth and development, organ morphogenesis, adversity stress and lipid metabolism. In addition, their potential applications in agriculture and industry are discussed.


GDSL lipase Structure Distribution Expression Biological functions 



We acknowledge financial support by Grant Nos. 2016YFD0101904 and 2016YFD0100305 from the National Key R&D Program of China, and 31471527 and 31271760 from the National Natural Science Foundation of China.


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Copyright information

© Franciszek Górski Institute of Plant Physiology, Polish Academy of Sciences, Kraków 2019

Authors and Affiliations

  • Li-Na Ding
    • 1
  • Ming Li
    • 1
  • Wei-Jie Wang
    • 1
  • Jun Cao
    • 1
  • Zheng Wang
    • 1
  • Ke-Ming Zhu
    • 1
  • Yan-Hua Yang
    • 1
  • Yu-Long Li
    • 1
  • Xiao-Li Tan
    • 1
    Email author
  1. 1.Institute of Life SciencesJiangsu UniversityZhenjiangChina

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