EC Number   |
Protein Variants |
Reference |
|---|
   3.4.21.41 | more |
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 |
81401 |
| 3.4.21.41 | 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 |
81391 |
| 3.4.21.41 | S654A |
mutant without autoactivation |
652680 |
| 3.4.21.41 | 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 |
652176 |
| 3.4.21.41 | R446Q |
stabilized in the single-chain proenzyme form by mutation at the cleavage site, no esterolytic activity with acetyl-Gly-Lys-methyl ester |
652176 |
| 3.4.21.41 | I306-C309del |
the deletion mutations are associated with periodontal Ehlers-Danlos syndrome |
752432 |
| 3.4.21.41 | R401-Y405del |
the deletion mutations are associated with periodontal Ehlers-Danlos syndrome |
752432 |
| 3.4.21.41 | R463X |
the mutants of the proenzyme Arg463Lys,Ile464Phe have increased stability, they retain their ability to autoactivate and have wild-type like hemolytic activity |
81405 |
| 3.4.21.41 | C309W |
the mutation is associated with periodontal Ehlers-Danlos syndrome |
752432 |
| 3.4.21.41 | C338R |
the mutation is associated with periodontal Ehlers-Danlos syndrome |
752432 |
