Abstract
1-aminocyclopropane-1-carboxylate oxidase (ACO) is the enzyme responsible for the final step in the biosynthesis of ethylene in flowering plants. At the Ethylene Conference that was held at Diepenbeek in 1988, Osborne [1] described the results of a survey of ethylene synthesis among lower plants. It revealed that all representatives of the major groups of non-flowering plants produced ethylene at detectable rates, but many plants were unable to convert 1-aminocyclopropane-1-carboxylate (ACC) to ethylene. Figure 1 shows the phylogenetic relationships among the groups of plants studied by Osborne [1] as deduced from analyses [2] of their 18S rRNA sequences, as in [3]. Mapping ACO onto this phylogeny suggests that ACO arose in a common ancestor of the groups represented today by the Cycads, Gymnosperms, Gnetales and Angiosperms, with more basal groups lacking the ability to convert ACC to ethylene. Speculation on the possible evolutionary origin of the ACO raises a host of questions, for which we currently have no answers. For example, the biochemical pathway by which lower plants produce ethylene remains unknown: in the aquatic fern, Regnellidium diphyllum, ACC is clearly not the substrate for ethylene production, and moreover ethylene is not derived from methionine [4].
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John, P. et al. (1997). 1-Aminocyclopropane-1-Carboxylate Oxidase: Molecular Structure and Catalytic Function. In: Kanellis, A.K., Chang, C., Kende, H., Grierson, D. (eds) Biology and Biotechnology of the Plant Hormone Ethylene. NATO ASI Series, vol 34. Springer, Dordrecht. https://doi.org/10.1007/978-94-011-5546-5_3
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DOI: https://doi.org/10.1007/978-94-011-5546-5_3
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