C2: EC 3.4.21.43
作者： Yuanyuan Xu , John E. Volanakis
DOI: 10.1016/B978-012733360-1/50014-2
关键词: Context (language use) 、 C3-convertase 、 Biochemistry 、 Enzyme 、 C5-convertase 、 Cleavage (embryo) 、 Protein subunit 、 Complement system 、 Serine protease 、 Chemistry
摘要: Publisher Summary This chapter describes C2, which is a single-polypeptide chain glycoprotein. C2 provides the catalytic subunit for C3 and C5 convertases of classical lectin pathways complement activation. Formation convertase requires Mg2+-dependent binding to activator-attached C4b subsequent cleavage by C1s or MASP. The C2a fragment remains bound expresses proteolytic activity against only in context C4b2a complex. Attachment C3b generates trimolecular complex C4b2a3b, convertase. Both enzymes share same active center provided serine protease domain C2a. restricted single-peptide bonds on C5, respectively.
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