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3.4.21.47: alternative-complement-pathway C3/C5 convertase

This is an abbreviated version!
For detailed information about alternative-complement-pathway C3/C5 convertase, go to the full flat file.

Word Map on EC 3.4.21.47

Reaction

Cleavage of Arg-/-Ser bond in complement component C3 alpha-chain to yield C3a and C3b, and Arg-/- bond in complement component C5 alpha-chain to yield C5a and C5b =

Synonyms

(C3b)n,Bb, (CVF)-dependent glycine-rich-beta-glucoprotein, alternative C3 convertase, alternative C5 convertase, alternative complement pathway C3 convertase, alternative complement pathway C3(C5) convertase, alternative pathway C3 convertase, alternative pathway C3 convertase complex, alternative pathway C3-convertase, alternative pathway C3/C5 convertase, alternative pathway C5 convertase, alternative pathway of complement C3/C5 convertase, alternative-complement-pathway C3/C5 convertase, AP C3 convertase, AP C3-convertase, AP C3/C5 convertase, AP C5 convertase, APC C3/C5 convertase, C3 convertase, C3 proactivator, C3/C5 convertase, C3b,Bb, C3b2, C3bB complex, C3bBb, C3bBb convertase, C3bBb(C3b)n, C3bBb3b, C3bBbC3b, C5 convertase, cobra venom factor-dependent C3 convertase, complement alternative pathway C3 convertase, complement C 3(C 5) convertase (amplification), complement C5 convertase, complement component C3/C5 convertase (alternative), convertase, complement C3(C5) (amplification), CVF,Bb, CVFh,Bb, CVFn,Bb, GBG, Glycine-rich beta glycoprotein, heat-labile factor, PBF2, proenzyme factor B, properdin factor B

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.21 Serine endopeptidases
                3.4.21.47 alternative-complement-pathway C3/C5 convertase

Engineering

Engineering on EC 3.4.21.47 - alternative-complement-pathway C3/C5 convertase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
923DELTADG
-
mutation in complement factor 3 gene identified in patients with dense deposit disease. Mutant C3923DELTADG, which lacks 2 amino acids, cannot be cleaved to C3b by the alternative pathway C3-convertase and is therefore the predominant circulating C3 protein in the patients. Upon activation to C3b by proteases, or to C3(H2O) by spontaneous thioester hydrolysis, mutant C3 generates an active C3-convertase that is regulated normally by decay accelerating factor but is resistant to decay by factor H. Activated C3b923DELTADG and C3(H2O)923DELTADG are resistant to proteolysis by factor I in the presence of factor H, but are efficiently inactivated in the presence of membrane cofactor protein, causing a fluid phase-restricted alternative pathway dysregulation in the patients that continuously activates and consumes C3 produced by the normal C3 allele
D254G
-
mutation in the Bb component decreases sensitivity to DAF to 9% of the wild-type value, sensitivity to CR1 to 4% of the wild-type value and sensitivity to Factor H to 48% of the wild-type value
D382A
-
mutation in the Bb component decreases sensitivity to DAF to 36% of the wild-type value, sensitivity to CR1 to 41% of the wild-type value
D382N
-
mutation in the Bb component decreases sensitivity to DAF to 54% of the wild-type value
D445A
-
mutation in the Bb component decreases sensitivity to CR1 to 71% of the wild-type value
D715A
-
factor B mutation, severly reduces hemolytic activity, in complex with C3b no cleavage of C3
D715E
-
factor B mutation, severly reduces hemolytic activity, in complex with C3b no cleavage of C3
D715N
-
factor B mutation, severly reduces hemolytic activity, in complex with C3b no cleavage of C3
D715S
-
factor B mutation, severly reduces hemolytic activity
D715Y
-
factor B mutation, severly reduces hemolytic activity
E207A
-
mutation in proenzyme factor B. Mutation disrupts salt bridge R234-E207, with little effects on the cleavage of proenzyme factor B
E301A
-
mutation in the Bb component decreases sensitivity to DAF to 75% of the wild-type value
E316A
-
mutation in the Bb component decreases sensitivity to DAF to 71% of the wild-type value
E379A
-
mutation in the Bb component decreases sensitivity to DAF to 52% of the wild-type value, sensitivity to CR1 to 50% of the wild-type value
E434A
-
mutation in the Bb component decreases sensitivity to CR1 to 65% of the wild-type value
E446V
-
mutation in proenzyme factor B. Mutation disrupts salt bridge R234-E446 which partly stabilizes the complex C3bB(Mg2+) thereby inhibiting activation of the proenzyme
F716A
-
factor B mutation, severly reduces hemolytic activity
K265A/K266A
-
Mutation in the Bb component decreases sensitivity to DAF to 18% of the wild-type value, sensitivity to CR1 to 18% of the wild-type value and sensitivity to Factor H to 19% of the wild-type value
K294A
-
mutation in the Bb component decreases sensitivity to CR1 to 44% of the wild-type value
M341A
-
mutation in the Bb component decreases sensitivity to Factor H to 75% of the wild-type value
N260D
-
mutation in the Bb component decreases sensitivity to DAF to 32% of the wild-type value, sensitivity to CR1 to 31% of the wild-type value and sensitivity to Factor H to 24% of the wild-type value
Q335A
-
mutation in the Bb component decreases sensitivity to DAF to 20% of the wild-type value
S339A
-
mutation in the Bb component decreases sensitivity to DAF to 32% of the wild-type value, sensitivity to CR1 to 50% of the wild-type value
W343A
-
mutation in the Bb component decreases sensitivity to DAF to 55% of the wild-type value, sensitivity to CR1 to 56% of the wild-type value
Y338A
-
mutation in the Bb component decreases sensitivity to DAF to 9% of the wild-type value, sensitivity to CR1 to 4% of the wild-type value and sensitivity to Factor H to 48% of the wild-type value
Y338F
-
mutation in the Bb component decreases sensitivity to DAF to 18% of the wild-type value, sensitivity to CR1 to 20% of the wild-type value and sensitivity to Factor H to 61% of the wild-type value
Y338S
-
mutation in the Bb component decreases sensitivity to DAF to 5% of the wild-type value, sensitivity to CR1 to 24% of the wild-type value
additional information