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Literature summary for 3.4.21.109 extracted from

  • Oberst, M.D.; Williams, C.A.; Dickson, R.B.; Johnson, M.D.; Lin, C.Y.
    The activation of matriptase requires its noncatalytic domains, serine protease domain, and its cognate inhibitor (2003), J. Biol. Chem., 278, 26773-26779.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
-
Homo sapiens

Protein Variants

Protein Variants Comment Organism
D482Y inhibited activation of matriptase Homo sapiens
D519Y inhibited activation of matriptase Homo sapiens
D555Y inhibited activation of matriptase Homo sapiens
D598Y inhibited activation of matriptase Homo sapiens
G149N results in production of only nonprocesse, full-lenth matriptase Homo sapiens
N109Q no reduced formation of matriptase-HAI-1-complex Homo sapiens
N302Q reduced formation of matriptase-HAI-1-complex Homo sapiens
N485Q no reduced formation of matriptase-HAI-1-complex Homo sapiens
N772Q reduced formation of matriptase-HAI-1-complex Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification one-chain zymogen is converted to an active two-chain protease, enzyme with mutation in its catalytic triad is unable to undergo this activational cleavage Homo sapiens