The Activity of a Type II Transmembrane Serine Protease, Matriptase, Is Dependent Solely on the Catalytic Domain

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  • KOJIMA Kenji
    Laboratory of Enzyme Chemistry, Division of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University
  • TSUZUKI Satoshi
    Laboratory of Nutrition Chemistry Division of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University
  • FUSHIKI Tohru
    Laboratory of Nutrition Chemistry Division of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University
  • INOUYE Kuniyo
    Laboratory of Enzyme Chemistry, Division of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University

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  • The activity of a type 2 transmembrane serine protease, matriptase, is dependent solely on the catalytic domain

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Abstract

Matriptase is a transmembrane serine protease comprising multiple domains in the extracellular region, including a stem domain and a catalytic domain. Using soluble matriptase variants containing entire extracellular domains or only the catalytic domain, the activity of this protease was found to depend solely on the catalytic domain. The stem domain had no significant effect on the activity.

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