Abstract
Luteolin, isolated from the seeds of Perilla frutescens (perilla seeds), inhibited the peroxidation of linoleic acid catalyzed by soybean lipoxygenase-1 (EC 1.13.11.12, Type 1) with an IC50 of 5.0 M (1.43 μg/mL) noncompetitively. The progress curves for an enzyme reaction indicate that luteolin shows slow binding kinetics. Both the initial velocity and steady-state rate in the progress curve were decreased with increasing the concentration of luteolin. The kinetic parameters, which described the inhibition by luteolin, were evaluated by nonlinear regression fits.
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References
Clapp, C. H., Banerjee, A., and Rotenberg, S. A., Inhibition of soybean lipoxygenase 1 by N-alkylhydroxylamines. Biochemistry, 24, 1826–1830 (1985).
Copeland, R. A., Enzyme: A practical introduction to structure, mechanism, and data analysis. Wiley-VCH, New York, (2000).
Cornicelli, J. A. and Trivedi, B. K., 15-Lipoxygenase and its inhibition: a novel therapeutic target for vascular disease. Curr. Pharm. Des., 5, 11–20 (1999).
Frieden, C., Kinetic aspects of regulation of metabolic processes. The hysteretic enzyme concept. J. Biol. Chem., 245, 5788–5799 (1970).
Gibian, M. J. and Galaway, R. A., Steady-state kinetics lipoxygenase oxygenation of unsaturated fatty acid. Biochemistry, 15, 4209–4214 (1976).
Grechkin, A., Recent developments in biochemistry of the plant lipoxygenase pathway. Prog. Lipid Res., 37, 317–352. (1998).
Ha T. J., Shimizu, K., Ogura, T., and Kubo, I., Inhibition mode of soybean lipoxygenase-1 by quercetin. Chem. Biodivers., 7, 1893–1903 (2010).
Jackson, W. P., Islip, J. P., Kneen, G., Pugh, A., and Wates, P. J., Acetohydroxamic acid as potent, selective, orally active 5-lipoxygenase inhibitors. J. Med. Chem., 31, 499–500 (1988).
Kemal, C., Louis-Flamberg, P., Krupinski-Olsen, R., and Shorter, A. L., Reductive inactivation of soybean lipoxygenase 1 by catechols: a possible mechanism for regulation of lipoxygenase activity. Biochemistry, 26, 7064–7072 (1987).
Kris-Etherton, P. M. and Keen, C. L., Evidence that the antioxidant flavonoids in tea and cocoa are beneficial for cardiovascular health. Curr. Opin. Lipidol., 13, 41–49 (2002).
Kwon, O. S., Choi, J. S., Islam, M. N., Kim, Y. S., and Kim, H. P., Inhibition of 5-lipoxygenase and skin inflammation by the aerial parts of Artemisia capillaris and its constituents. Arch. Pharm. Res., 34, 1561–1569 (2011).
Makino, H., Furata, Y., Fujii, H., Nakagawa, T., Wakushima, H., Saito, K., and Kano, Y., Effect of oral treatment of Perilla frutescens and its constituents on type-I allergy in mice. Biol. Pharm. Bull., 24, 1206–1209 (2001).
Makino, H., Furata, Y., Wakushima, H., Fujii, H., Saito, K., and Kano, Y., Anti-allergic effect of Perilla frutescens and its active constituents. Phytother. Res., 17, 240–243 (2003).
Makino, T., Ono, T., Muso, E., and Honda, G., Effect of Perilla frutescens on nitric oxide production and DNA synthesis in cultured murine vascular smooth muscle cells. Phytother. Res., 16, S19–S23 (2002).
Mansuy, D., Cucurou, C., Biatry, B., and Battioni, J. P., Soybean lipoxygenase-catalyzed oxidations by linoleic acid hydroperoxide: different reducing substrates and dehydrogenation of phenidone and BW 755C. Biochem. Biophys. Res. Commun., 151, 339–346 (1988).
Morrison, J. F., The slow binding and slow, tight binding inhibition of enzyme catalyzed reaction. Trends Biochem. Sci., 7, 102–107 (1982).
Morrison, J. F. and Walsh, C. T., The behaviors and significance of slow binding enzyme inhibitors. Adv. Enzymol. Relat. Areas Mol. Biol., 61, 201–302 (1988).
Nakamura, Y., Ohto, Y., Murakami, A., and Ohigashi, H., Superoxide scavenging activity of rosmarinic acid from Perilla frutescens Britton var. acuta f. viridis. J. Agric. Food Chem., 46, 4545–4550 (1998).
Nelson, M. J., Catecholate complex of ferric soybean lipoxygenase 1. Biochemistry, 27, 4273–4278 (1988).
Richard-Forget, F., Gauillard, F., Hugues, M., Jean-Marc, T., Boivin, P., and Nicolas, J., Inhibition of horse bean and germinated barley lipoxygenases by some phenolic compounds. J. Food Sci., 60, 1325–1329 (1995).
Rickert, K. W. and Klinman, J. P., Nature of hydrogen transfer in soybean lipoxygenase 1: separation of primary and secondary isotope effects. Biochemistry, 38, 12218–12228 (1999).
Riendeau, D., Falgueyret, J.-P., Guay, J., Ueda, N., and Yamamoto, S., Pseudoperoxidase activity of 5-lipoxygenase stimulated by potent benzofuranol and N-hydroxyurea inhibitors of the lipoxygenase reaction. Biochem. J., 274, 287–292 (1991).
Sadik, C. D., Sies, H., and Schewe, T., Inhibition of 15-lipoxygenase by flavonoids: structure-activity relations and mode of action. Biochem. Pharmacol., 65, 773–781 (2003).
Summers, J. B., Mazdiyasni, H., Holms, J. H., Ratajczyk, J. D., Dyer, R. D., and Carter, G. W., Hydroxamic acid inhibitors of 5-lipoxygenase. J. Med. Chem., 30, 574–580 (1987).
Yamamoto, H., Sakakibara, J., Nagatsu, A., and Sekiya, K., Inhibitors of arachidonate lipoxygenase from defatted perilla seed. J. Agric. Food Chem., 46, 862–865 (1998).
Yamasaki, K., Nakano, M., Kawahata, T., Mori, H., Otaka, T., Ueba, N., Oishi, I., Inami, R., Yamane, M., Nakamura, M., Murata, H., and Nakanishi, T., Anti-HIV-1 activity of herbs in Labiatae. Biol. Pharm. Bull., 21, 829–833 (1998).
Yoshimoto, T., Furukawa, M., Yamamoto, S., Horie, T., and Watanabe-Kohno, S., Flavonoids: potent inhibitors of arachidonate 5-lipoxygenase. Biochem. Biophys. Res. Commun., 116, 612–618 (1983).
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Ha, T.J., Lee, MH., Kim, HT. et al. Slow-binding inhibition of soybean lipoxygenase-1 by luteolin. Arch. Pharm. Res. 35, 1811–1816 (2012). https://doi.org/10.1007/s12272-012-1014-x
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DOI: https://doi.org/10.1007/s12272-012-1014-x