The activity of a type II transmembrane serine protease, matriptase, is dependent solely on the catalytic domain.
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.
Kojima
Kenji
K
Laboratory of Enzyme Chemistry, Division of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University, Japan.
Tsuzuki
Satoshi
S
Fushiki
Tohru
T
Inouye
Kuniyo
K
D000595:Amino Acid Sequence; D000818:Animals; D016466:CHO Cells; D020134:Catalytic Domain; D003374:Coumarins / Q000378:metabolism; D006224:Cricetinae; D003412:Cricetulus; D006801:Humans; D008969:Molecular Sequence Data; D009154:Mutation; D051381:Rats; D012697:Serine Endopeptidases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*
C502573:4-methyl-coumaryl-7-amide; D003374:Coumarins; D012697:Serine Endopeptidases; C485595:matriptase