Publication: Structural basis for reduced activity of 1-aminocyclopropane-1-carboxylate synthase affected by a mutation linked to andromonoecy
Structural basis for reduced activity of 1-aminocyclopropane-1-carboxylate synthase affected by a mutation linked to andromonoecy
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Schärer, M. A., Eliot, A. C., Grütter, M. G., & Capitani, G. (2011). Structural basis for reduced activity of 1-aminocyclopropane-1-carboxylate synthase affected by a mutation linked to andromonoecy. FEBS Letters, 585(1), 111–114. https://doi.org/10.1016/j.febslet.2010.11.013
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1-aminocyclopropane-1-carboxylate synthase (ACS) is a key enzyme in the biosynthesis of the plant hormone ethylene. Recently, a new biological role for ACS has been found in Cucumis melo where a single point mutation (A57V) of one isoform of the enzyme, causing reduced activity, results in andromonoecious plants. We present here a straightforward structural basis for the reduced activity of the A57V mutant, based on our work on Malus domestica ACS, including a new structure of the unliganded apple enzyme at 1.35Å resolution.
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- Schärer, M A
- Eliot, A C
- Grütter, M G
- Capitani, G
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Schärer, M. A., Eliot, A. C., Grütter, M. G., & Capitani, G. (2011). Structural basis for reduced activity of 1-aminocyclopropane-1-carboxylate synthase affected by a mutation linked to andromonoecy. FEBS Letters, 585(1), 111–114. https://doi.org/10.1016/j.febslet.2010.11.013
