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Molecular Pharmacology, Vol 13, 362-367, Copyright © 1977 by the American Society for Pharmacology and Experimental Therapeutics

Inhibition of Two Copper-Containing Enzymes, Tyrosinase and Dopamine beta-Hydroxylase, by L-Mimosine

HIDEO HASHIGUCHI 1 and HITOSHI TAKAHASHI 1

1 Department of Biochemistry, Toxicology Institute, Kumamoto University Medical School, Kumamoto, Japan

Because of the structural similarity of L-mimosine to L-tyrosine and L-dopa and its tendency to chelate cupric ion, the influence of this compound on mammalian tyrosinase from mouse melanoma and dopamine beta-hydroxylase extracted from bovine adrenal medulla was investigated in vitro. L-Mimosine inhibited tyrosinase competitively and reversibly, and the inhibitory effect was decreased by ferric, aluminum, or cupric ion. Dopamine beta-hydroxylase was inhibited by L-mimosine, mimosinamine, and mimosinic acid, but the inhibition was uncompetitive. The results suggest that these enzymes are inhibited by different mechanisms: L-mimosine inhibits tyrosinase because of its structural similarity to the substrate, L-dopa. Dopamine beta-hydroxylase is inhibited by L-mimosine, mimosinamine, and mimosinic acid because of their chelate-forming ability.

Note:
ACKNOWLEDGMENTS The authors express their deep thanks to Dr. T. Ohuchi for his helpful advice, and Miss K. Ueda for her technical assistance in the enzyme assays.

Submitted on March 5, 1976
Accepted on November 9, 1976




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Copyright © 1977 by the American Society for Pharmacology and Experimental Therapeutics