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3.4.21.45: complement factor I

This is an abbreviated version!
For detailed information about complement factor I, go to the full flat file.

Word Map on EC 3.4.21.45

Reaction

Inactivates complement subcomponents C3b, iC3b and C4b by proteolytic cleavage =

Synonyms

C3b inactivator, C3b/C4b inactivator, C3bINA, CFI, complement C3b inactivator, complement C3b/C4b inactivator, complement C4b inactivator, complement C4bi, complement compoment C3b inactivator, complement factor I, complement inhibitor factor I, complement regulator factor I, conglutinogen-activating factor C, factor I, factor I-like activity, fI, GcIf-1, GcIf-2, GcIf-3, GcIf-4, IF, plasma protease factor I, serine protease Factor I

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.21 Serine endopeptidases
                3.4.21.45 complement factor I

Molecular Weight

Molecular Weight on EC 3.4.21.45 - complement factor I

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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
155000
-
gel filtration
1622
A2G2, deduced molecular weight of N-linked glycan structure
1824
A3G2, deduced molecular weight of N-linked glycan structure
1912
A2G2S1, deduced molecular weight of N-linked glycan structure
2115
A3G2S1, deduced molecular weight of N-linked glycan structure
2202
A2G2S2, deduced molecular weight of N-linked glycan structure
2277
A3G3S1, deduced molecular weight of N-linked glycan structure
2405
A3G2S2, deduced molecular weight of N-linked glycan structure
2567
A3G3S2, deduced molecular weight of N-linked glycan structure
27000
-
1 * 27000 + 1 * 37500, calculation from nucleotide sequence
27590
calculated for non-glycosylated light chain, estimated basing upon results of the N-linked glycan analysis
28500
-
1 * 28500 + 1 * 38000, calculation from nucleotide sequence
30270
estimated for light chain of a partially deglycosylated factor I bearing a single N-linked Man3GlcNAc2 core structure at each glycosylation site
35290
calculated for non-glycosylated heavy chain, estimated basing upon results of the N-linked glycan analysis
3569
approximate reduction of molecular weight for the heavy chain after partial deglycosylation of native protein with ABS, BTG and GuH exoglycosidases
35900
native light chain, estimated basing upon results from the N-linked glycan analysis
37000
light chain of
37500
-
1 * 27000 + 1 * 37500, calculation from nucleotide sequence
37960
estimated for heavy chain of a partially deglycosylated factor I bearing a single N-linked Man3GlcNAc2 core structure at each glycosylation site
38000
41530
native heavy chain, estimated basing upon results from the N-linked glycan analysis
50000
5632
approximate reduction of molecular weight for the light chain after partial deglycosylation of native protein with ABS, BTG and GuH exoglycosidases
58000
-
SDS-PAGE
62880
total calculated molecular weight for non-glycosylated factor I, estimated basing upon results of the N-linked glycan analysis
66000
-
nonglycosylated proenzyme
68230
estimated for total protein bearing a single N-linked Man3GlcNAc2 core structure at each glycosylation site
75000
-
x * 75000, SDS-PAGE
77430
deduced for total protein of the native factor I basing upon results from the N-linked glycan analysis
892
Man3GlcNAc2 core, deduced molecular weight of N-linked glycan structure
90000
9201
approximate reduction of molecular weight for total molecule of factor I after partial deglycosylation of native protein with ABS, BTG and GuH exoglycosidases
additional information
mutant protein reveals a slightly different migration pattern during electrophoresis under reducing conditions, due to proximity of the mutation to a cysteine residue