Anisaldehyde characterized in the seeds of Pimpinella anisum L. (Umbelliferae), also known as aniseed, was found to inhibit the oxidation of l -3,4-dihydroxyphenylalanine ( l -DOPA) by mushroom tyrosinase (EC 1.14.18.1) with an ID 50 of 43 μg/mL (0.32 mM). The inhibition kinetics analyzed by a Lineweaver−Burk plot established anisaldehyde to be a noncompetitive inhibitor for this oxidation. On the basis of this finding, various related analogues were also tested in order to gain new insights into their structural functions.
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Kubo et al. (1998) studied this question.
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