In vitro and in vivo evidence for oxalate oxidase activity of a germin-like protein from azalea

Atsushi Sakamoto, Takashi Nishimura, Yoh Ichi Miyaki, Shunsuke Watanabe, Hiroshi Takagi, Shunsuke Izumi, Hiroshi Shimada

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18 Scopus citations


Germins and germin-like proteins (GLPs) comprise large families of extracellular plant glycoproteins that are structurally similar, yet they have been reported to have distinct biochemical activities: oxalate oxidase and superoxide dismutase activities, respectively. We expressed an azalea GLP (RmGLP2) in cultured cells of tobacco, and determined that the extracellular protein fraction and the recombinant RmGLP2 protein purified from these cells catalyzed the oxidation of oxalate. Notably, this activity is purportedly restricted to germin and has not been demonstrated for a GLP. Although the specific activity of the purified RmGLP2 protein was low compared with that of a previously characterized barley germin/oxalate oxidase, tobacco cells expressing RmGLP2 exhibited significantly reduced oxalate levels. Thus, RmGLP2 represents the first reported GLP with oxalate oxidase activity.

Original languageEnglish (US)
Pages (from-to)536-542
Number of pages7
JournalBiochemical and Biophysical Research Communications
Issue number3
StatePublished - Mar 13 2015

Bibliographical note

Publisher Copyright:
© 2015 Elsevier Inc. All rights reserved.


  • Cupin
  • Extracellular matrix protein
  • Germin-like protein
  • Hydrogen peroxide
  • Oxalate oxidase
  • Superoxide dismutase


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