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II型跨膜丝氨酸蛋白酶胃蛋白酶的活性仅取决于催化结构域。

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

作者信息

Kojima Kenji, Tsuzuki Satoshi, Fushiki Tohru, Inouye Kuniyo

机构信息

Laboratory of Enzyme Chemistry, Division of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University, Japan.

出版信息

Biosci Biotechnol Biochem. 2009 Feb;73(2):454-6. doi: 10.1271/bbb.80713. Epub 2009 Feb 7.

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.

摘要

Matriptase是一种跨膜丝氨酸蛋白酶,其细胞外区域包含多个结构域,包括一个茎状结构域和一个催化结构域。使用包含整个细胞外结构域或仅催化结构域的可溶性matriptase变体,发现这种蛋白酶的活性仅取决于催化结构域。茎状结构域对活性没有显著影响。

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