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Results 1 - 7 of 7
EC Number
Amino acid exchange
Commentary
Reference
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by the point mutation of C1r - Arg-Phe - of the natural cleavage site Arg-Ile - the zymogen is stabilized, while the biological activity is not affected
R446Q
stabilized in the single-chain proenzyme form by mutation at the cleavage site, no esterolytic activity with acetyl-Gly-Lys-methyl ester
R463X
construction of a stable zymogen by mutating the Arg463Ile bond shows that one active C1r in the C1 complex is sufficient for the full activity of the entire complex
R463X
the mutants of the proenzyme Arg463Lys,Ile464Phe have increased stability, they retain their ability to autoactivate and have wild-type like hemolytic activity
R463X
the mutations Arg463Gln, Arg463Lys or Arg463Phe all stabilize the zymogen state
S637A
stabilized in the single-chain proenzyme form by mutation at the active site serine residue, no esterolytic activity with acetyl-Gly-Lys-methyl ester
S654A
mutant without autoactivation
Results 1 - 7 of 7