3.4.21.41: complement subcomponent C1r
This is an abbreviated version!
For detailed information about complement subcomponent C1r, go to the full flat file.
Reaction
Selective cleavage of Lys(or Arg)-/-Ile bond in complement subcomponent C1s to form C_overbar_1s_ (EC 3.4.21.42) =
Synonyms
activated complement C1r, C1r, C1r protease, C1r serine protease, C1r-LP, C1rbar-esterase, complement C1r subcomponent-like protein, complement C1r, activated, complement protease C1r, complement subcomponent 1r, CUB, multiprotein complex C1, proteases C1r, serine protease C1r, Xld, xolloid
ECTree
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Engineering
Engineering on EC 3.4.21.41 - complement subcomponent C1r
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I306-C309del
the deletion mutations are associated with periodontal Ehlers-Danlos syndrome
R401-Y405del
the deletion mutations are associated with periodontal Ehlers-Danlos syndrome
R446Q
-
stabilized in the single-chain proenzyme form by mutation at the cleavage site, no esterolytic activity with acetyl-Gly-Lys-methyl ester
R463X
S637A
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stabilized in the single-chain proenzyme form by mutation at the active site serine residue, no esterolytic activity with acetyl-Gly-Lys-methyl ester
additional information
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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
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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
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the mutants of the proenzyme Arg463Lys,Ile464Phe have increased stability, they retain their ability to autoactivate and have wild-type like hemolytic activity
R463X
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the mutations Arg463Gln, Arg463Lys or Arg463Phe all stabilize the zymogen state