Poster Presentation The 42nd Lorne Conference on Protein Structure and Function 2017

Structural and inhibition studies of 1-aminocyclopropane-1-carboxylic acid oxidase (#144)

Dona Gunawardana 1 , John Arabshahi 1 , Yuliana Yosaatmadja 2 , Johannes Reynisson 1 , Christopher Squire 2 , Ivanhoe Leung 1
  1. School of Chemical Sciences, University of Auckland, Auckland, New Zealand
  2. School of Biological Sciences , University of Auckland, Auckland, New Zealand

 

Ethylene is an essential plant hormone that regulates plant growth and development. Two enzymes are involved in the plant ethylene biosynthesis pathway, including 1-aminocycloproape-1-carboxylate oxidase (ACCO), which catalyses the conversion of 1-aminocycloproape-1-carboxylate (ACC) into ethylene.1,2 The ethylene biosynthesis pathway, including ACCO, is a current inhibition target for plant growth regulators.3 However, progress to date has been, at least in part, hampered by the lack of structural information about substrate binding at the ACCO active site.

Herein, we report our progress in the structural characterisation of ACCO by using petunia hybrida as a model system. Virtual screening was applied to identify potential ACCO inhibitors. We have also developed and optimised a nuclear magnetic resonance (NMR)-based binding technique for the screening and quantification of ACCO inhibitors. Overall, our results pave way and provide a basis for future development of plant regulators that target ACCO.

  1. 1. Yang, S. F.; Hoffman, N. E. Ethylene biosynthesis and its regulation in higher plants. Ann. Rev. Plant Physiol. 1984, 35, 155–189.
  2. 2. Zhang, Z.; Ren, J.-S.; Clifton, I. J.; Schofield, C. J. Crystal structure and mechanistic
  3. 3. Martínez-Romero, D.; Bailén, G.; Serrano, M.; Guillén, F.; Valverde, J. M.; Zapata, P.; Castillo, S.; Valero, D. Tools to maintain postharvest fruit and vegetable quality through the inhibition of ethylene action: a review. Crit. Rev. Food Sci. Nutr. 2007, 47, 543–560.