Laccase-catalyzed tyrosine click reaction with 1-methyl-4-arylurazole: rapid labeling on protein surfaces

  • Chem Commun (Camb). 2024 Nov 28;60(96):14208-14211. doi: 10.1039/d4cc03802a.
Keita Nakane  1  2 ,  Chizu Fujimura  1 ,  Shogo Miyano  2 ,  Zhengyi Liu  1 ,  Tatsuya Niwa  3 ,  Hafumi Nishi  4  5  6 ,  Tetsuya Kadonosono  7 ,  Hideki Taguchi  3 ,  Shusuke Tomoshige  2 ,  Minoru Ishikawa  2 ,  Shinichi Sato  1  2
Affiliations
  • 1. Frontier Research Institute for Interdisciplinary Sciences, Tohoku University, 6-3 Aramaki aza-Aoba, Aoba-ku, Sendai, Miyagi 980-8578, Japan. [email protected].
  • 2. Graduate School of Life Sciences, Tohoku University, 2-1-1 Katahira, Aoba-ku, Sendai, Miyagi 980-8577, Japan.
  • 3. Cell Biology Center, Institute of Innovative Research, Tokyo Institute of Technology, 4259-S2-19, Nagatsuta-cho, Midori-ku, Yokohama, Kanagawa 226-8501, Japan.
  • 4. Department of Applied Information Sciences, Graduate School of Information Sciences, Tohoku University, 6-3 Aramaki Aza-Aoba, Aoba-ku, Sendai, Miyagi 980-8578, Japan.
  • 5. Tohoku Medical Megabank Organization, Tohoku University, 2-1 Seiryo-machi, Aoba-ku, Sendai, Miyagi 980-8573, Japan.
  • 6. Faculty of Core Research, Ochanomizu University, 2-1-1 Otsuka, Bunkyo-ku, Tokyo 112-8610, Japan.
  • 7. School of Life Science and Technology, Tokyo Institute of Technology, Yokohama, Kanagawa 226-8501, Japan.
PMID: 39531010 DOI: 10.1039/d4cc03802a
Abstract

Our study demonstrates the exceptional efficiency of 1-methyl-4-arylurazole (MAUra) for tyrosine labeling, optimized with laccase under mild conditions, achieving a high efficiency (kcat/Km = 7.88 × 104 M-1 s-1) with minimal oxidative side reactions and selective labeling of highly exposed tyrosine sites on proteins.

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