Abstract
The paper concerns two aspects of the role of 1-aminocyclopropane-1-carboxylate oxidase (ACO) in the biosynthesis of ethylene. First, a mechanism is proposed to account for the provision of ascorbate to the enzyme functioning in the plant cell. Evidence indicates that the enzyme is located in the apoplasm, at least in ripening fruit. It is suggested that ascorbate in the apoplast remains in a reduced state by the outward flow of reducing potential across the plasma membrane. Second, ACO is proposed to have evolved from an ancestral Fe (II)-dependent dioxygenase so as to enhance ethylene production as a regulated signal of plant stress. Among extant non-flowering plants, ACO activity has been found only in seedlings of representatives of the Coniferales and Gnetales. These results suggest that ACO arose relatively late in the evolution of the land plants; an evolutionary event reversed by suppressing expression in genetically engineered fruits.
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© 1999 Springer Science+Business Media Dordrecht
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John, P., Reynolds, E.A., Prescott, A.G., Bauchot, AD. (1999). ACC Oxidase in the Biosynthesis of Ethylene. In: Kanellis, A.K., Chang, C., Klee, H., Bleecker, A.B., Pech, J.C., Grierson, D. (eds) Biology and Biotechnology of the Plant Hormone Ethylene II. Springer, Dordrecht. https://doi.org/10.1007/978-94-011-4453-7_1
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DOI: https://doi.org/10.1007/978-94-011-4453-7_1
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