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Limulus clotting factor C
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<p>Limulus clotting factor overbar C (<a href="/facts/Enzyme_Commission_number/Y5GNLRKX">EC</a> <a href="https://enzyme.expasy.org/EC/3.4.21.84">3.4.21.84</a>, <i>factor C</i>, <i>limulus factor C</i>) is an <a href="/facts/Enzyme/DSI1Fh7y">enzyme</a>. This enzyme <a href="/facts/Catalysis/LPBS7TQC">catalyses</a> the following <a href="/facts/Chemical_reaction/GpqWlKrz">chemical reaction</a> </p> Selective cleavage of -Arg103-Ser- and -Ile124-Ile- bonds in <a href="/facts/Limulus_clotting_factor_B/SR0UYFaF">limulus clotting factor B</a> to form <i>factor overbar B</i>. Cleavage of -Pro-Arg- bonds in synthetic substrates <p>This enzyme is isolated from the <a href="/facts/Hemocyte/lf9GA0Dj">hemocyte</a> granules of the <a href="/facts/Horseshoe_crab/IuaBGa9T">horseshoe crabs</a> <a href="/facts/Limulus/QT4e4wkd">Limulus</a> and <a href="/facts/Tachypleus/LjP4qRTc">Tachypleus</a>, where it serves as a LPS endotoxin-sensitive <a href="/facts/Trypsin/wrwS23rh">trypsin</a> type <a href="/facts/Serine_protease/kGfEE6hE">serine protease</a> to protect the <a href="/facts/Organism/j8JkL09u">organism</a> from <a href="/facts/Bacteria/wC8xSCsU">bacterial</a> infection, initiating a cascade leading to <a href="/facts/Coagulin/UDGrf8pn">coagulin</a> formation. From the N-terminus to the C-terminus, the domains are: </p> <ul><li><a href="/facts/Epidermal_growth_factor_family/hzls9ypa">EGF-like</a> domain</li> <li>3 <a href="/facts/Sushi_domain/kjjtV428">Sushi domains</a></li> <li>one <a href="/facts/LCCL_domain/rxsdvubb">LCCL domain</a> and one <a href="/facts/C-type_lectin/4ALDM3dm">C-type lectin</a> domain</li> <li>2 more Sushi domains</li> <li>a trypsin domain</li></ul> <p>This enzyme is useful in <a href="/facts/Limulus_amebocyte_lysate/M5BmAkYR">Limulus amebocyte lysate</a> as the endotoxin-detecting element. It can be produced recombinantly. </p>