Literature summary for 3.4.21.47 extracted from

Koelln, J.; Spillner, E.; Andrae, J.; Klensang, K.; Bredehorst, R.
Complement inactivation by recombinant human C3 derivatives (2004), J. Immunol., 173, 5540-5545.

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Application

Application	Comment	Organism
medicine	therapeutic reduction of complement activity in vivo by use of engineered enzyme component C3 resulting in greatly improved half-life of C3 convertase	Homo sapiens

Protein Variants

Protein Variants	Comment	Organism
additional information	substitution of enzyme component C3 domains by corresponding domains of cobra venom factor. Structural domains of cobra venom factor gamma- or beta-chains confer stability to C3 convertase complex. Replacement of terminal C-275 amino acids by those of cobra venom factor beta-chain results in a catalytic activity of C3 convertase similar to wild-type, but with a half-life of 5-6 h compared to 1-2 min for wild-type	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	recombinant enzyme component C3	-

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Release 2023.1 (January 2023)