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. 2013 Aug 1;5:plt031. doi: 10.1093/aobpla/plt031

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Published by Oxford University Press on behalf of the Annals of Botany Company

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/3.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.

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Figure 2. — Ser246 and Arg244 are ACC binding sites in ACCO. Thr157 is essential for ACCO activity in a protein structure role. The ACC K_m is greatly elevated for the Ser246Ala and Arg244Lys mutants. The standard assay was employed using crude lysate with ACC varied. ACC oxidase activity is virtually non-detectable for the triple mutant (Ser246Ala/Arg244Lys/Thr157Ala).