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Updated: Sep 30, 2026

Quantification of Hypopigmentation Activity In Vitro
Published on: March 6, 2019
Inhibition of transglutaminase by synthetic tyrosine melanin
Koji Ikura1, Chiemi Otomo, Shunji Natsuka
1Department of Applied Biology, Kyoto Institute of Technology, Matsugasaki, Japan. ikura@ipc.kit.ac.jp
Abstract:
Transglutaminases catalyze the cross-linking and amine incorporation of proteins, and are implicated in various biological phenomena. Previously, we found a high molecular mass transglutaminase-inhibitory substance produced by Streptomyces lavendulae Y-200 that appeared to be a melanin substance. Here, we report that synthetic tyrosine melanin inhibited various types of transglutaminases. Tyrosine melanin inhibited tissue-type transglutaminase in a competitive manner with a glutamine substrate, and also inhibited the cross-linking of casein catalyzed by a tissue-type transglutaminase. The melanized hemolymph of the silkworm and melanin solutions prepared from melanin precursors inhibited tissue-type transglutaminase. These results suggested that the melanin substances generally inhibit transglutaminases.
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