Structural Features Required for Inhibition of Soybean Lipoxygenase-2 by Propyl Gallate 1: Evidence that Lipoxygenase Activity Is Distinct from the Alternative Pathway (original) (raw)

Abstract

The ability of 19 structural analogs of propyl gallate to inhibit purified soybean seed (Glycine max [L.] Merr. var. Ransom) lipoxygenase-2 (EC 1.13.11.12) was determined. The results indicate that the _o_-dihydroxy and not the ester function of propyl gallate is essential for inhibition of lipoxygenase. Catechol thus represents the minimum inhibitory structure. Among those compounds possessing an _o_-dihydroxy function, the _Ki_′ for inhibition of lipoxygenase is directly related to the lipophilicity of the inhibitor as measured by the octanol-water partition coefficient. The structural features of propyl gallate necessary for inhibition of lipoxygenase were found to differ from those required for inhibition of the plant mitochondrial alternative pathway. This further supports the concept that the alternative oxidase and lipoxygenase are functionally distinct species.

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This investigation was supported by a grant from the National Institute of General Medical Sciences (United States Public Health Service GM 26095) to J. N. S.

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© 1983 American Society of Plant Biologists

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