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Literature summary for 3.4.22.B65 extracted from

  • Hassanein, M.; Bojja, A.S.; Glazewski, L.; Lu, G.; Mason, R.W.
    Protein processing by the placental protease, cathepsin P (2009), Mol. Hum. Reprod., 15, 433-442.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expression in Pichia pastoris Mus musculus

Organism

Organism UniProt Comment Textmining
Mus musculus Q9R014
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-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
calreticulin + H2O endoplasmic reticulum protein substrate identified by incubation of recombinant enzyme with rat choriocarcinoma cell proteins Mus musculus ? protein is processed from the C-terminus, with removal of the KDEL endoplasmic reticulum retention signal. Cathepsin L co-localizes with calreticulin in rat choriocarcinoma cell ?
Gp96 protein + H2O endoplasmic reticulum protein substrate identified by incubation of recombinant enzyme with rat choriocarcinoma cell proteins Mus musculus ? protein is sequentially processed by cathepsin P at 2 sites towards the C-terminus of the protein, with removal of the KDEL endoplasmic reticulum retention signal. Cathepsin L co-localizes with gp96 in rat choriocarcinoma cell ?