Tarantula hemocyanin shows phenoloxidase activity.

@article{Decker1998TarantulaHS,
  title={Tarantula hemocyanin shows phenoloxidase activity.},
  author={Heinz Decker and T. Rimke},
  journal={The Journal of biological chemistry},
  year={1998},
  volume={273 40},
  pages={25889-92}
}
An enzyme generally catalyzes one well defined reaction with high specificity and efficiency. We report here in contrast that the copper protein hemocyanin of the tarantula Eurypelma californicum exhibits two different functions. These occur at the same active site. While hemocyanin usually is an oxygen carrier, its function can be transformed totally to monophenoloxidase and o-diphenoloxidase activity after limited proteolysis with trypsin or chymotrypsin. N-acetyldopamine (NADA) is more… CONTINUE READING

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