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Results 1 - 10 of 27 > >>
EC Number Protein Variants Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.42C1s(MASP-2 CCP1/2) chimeric C1s protease containing the MASP-2 complement control protein domain, cleavage efficiency of C4 similar to MASP-2 protease 665686
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.42C1s(MASP-2 SP) chimeric C1s protease containing the MASP-2 serine protease domain, cleavage efficiency similar to wild-type C1s 665686
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.42C294R the mutation is associated with periodontal Ehlers-Danlos syndrome 752432
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.42D275S/P276I/K405V similar to wild-type C1s 665686
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.42D343N complement component C4 cleavage activity below 50% compared to wild-type, complement component C2 cleavage activity similar to wild-type 669727
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.42G630E missense mutation, like normal C1s, the mutant has the ability to form a complex with rC1r. The activity of the mutant is significantly lower than that of wild-type, being only 60% of the activity of the wild-type rC1s. The mutant has a higher susceptibility to proteolysis than the wild-type, and prolonged proteolysis generates a truncated L chain with little or no protease activity 699344
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.42K628A the mutant shows lower activity than wild-type enzyme against peptide substrates, cleavage of C4 is reduced by 5fold compared to the wild-type enzyme 731865
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.42K628Q the mutant shows greater activity than wild-type enzyme against peptide substrates and peptide substrates containing physiological substrate sequences, unaltered activity with 2-aminobenzoyl-GLQRALEI-Lys(dinitrophenol)-NH2 substrate compared to the wild-type enzyme, but cleavage of C4 complement is reduced by 5fold compared to the wild-type enzyme 731865
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.42more only the fragment bearing the serine protease (SP) and the complement control protein (CCP) module 2 of MASP-2 were expressed and crystallized 659718
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.42P341I complement component C4 cleavage activity below 50% compared to wild-type, complement component C2 cleavage activity similar to wild-type 669727
Results 1 - 10 of 27 > >>