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Literature summary for 3.4.21.45 extracted from

  • Sanchez-Gallego, J.I.; Groeneveld, T.W.; Krentz, S.; Nilsson, S.C.; Villoutreix, B.O.; Blom, A.M.
    Analysis of binding sites on complement factor I using artificial N-linked glycosylation (2012), J. Biol. Chem., 287, 13572-13583.
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
C4b binding protein C4BP, required for activity, dependent on Homo sapiens
factor H required for activity, dependent on Homo sapiens

Protein Variants

Protein Variants Comment Organism
D104S site-directed mutagenesis, altered kinetics compared to the wild-type Homo sapiens
D385N/K387S site-directed mutagenesis, altered kinetics compared to the wild-type Homo sapiens
D420N/N422T site-directed mutagenesis, the mutation in the serine protease domain decreases the binding of the enzyme to substrate analogue C3met Homo sapiens
D497N site-directed mutagenesis, altered kinetics compared to the wild-type Homo sapiens
F82N/N84T site-directed mutagenesis, the mutation in the FIMAC domain impairs enzyme activity, which is rescued by deglycosylation of the mutant Homo sapiens
K124N site-directed mutagenesis, altered kinetics compared to the wild-type Homo sapiens
K182N/R184S site-directed mutagenesis, altered kinetics compared to the wild-type Homo sapiens
K326N/A328T site-directed mutagenesis, the mutation in the serine protease domain decreases the binding of the enzyme to substrate analogue C3met Homo sapiens
K458N/N460T site-directed mutagenesis, altered kinetics compared to the wild-type Homo sapiens
L171N site-directed mutagenesis, altered kinetics compared to the wild-type Homo sapiens
additional information mutations in the FIMAC, CD5, and LDLr1 domains do not decrease the binding of the enzyme to substrate analogues C3met or C4met Homo sapiens
N404T site-directed mutagenesis, the mutation in the serine protease domain decreases the binding of the enzyme to substrate analogues C3met and C4met Homo sapiens
Q210N/V212T site-directed mutagenesis, altered kinetics compared to the wild-type Homo sapiens
Q219N/K221S site-directed mutagenesis, altered kinetics compared to the wild-type Homo sapiens
Q242N/K244S site-directed mutagenesis, the mutation in the LDLr2 domain decreases the binding of the enzyme to substrate analogues C3met and C4met Homo sapiens
Q257N/Q259S site-directed mutagenesis, the mutation in the LDLr2 domain decreases the binding of the enzyme to substrate analogues C3met and C4met Homo sapiens
R35N/I37T site-directed mutagenesis, the mutation in the FIMAC domain impairs enzyme activity, which is rescued by deglycosylation of the mutant Homo sapiens
R365N site-directed mutagenesis, the mutation in the serine protease domain decreases the binding of the enzyme to substrate analogues C3met and C4met Homo sapiens
R61N site-directed mutagenesis, altered kinetics compared to the wild-type Homo sapiens
S561N/Y563T site-directed mutagenesis, the mutation in the serine protease domain impairs enzyme activity, which is rescued by deglycosylation of the mutant Homo sapiens
T54N/V56T site-directed mutagenesis, altered kinetics compared to the wild-type Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
additional information the enzyme does not have any known physiological inhibitor, although synthetic inhibitors, such as suramin, are able to weakly inhibit it Homo sapiens
suramin weak inhibition Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular the enzyme circulates in the blood Homo sapiens
-
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
38000
-
1 * 50000 + 1 * 38000, SDS-PAGE, the enzyme is proteolytically processed into the heavy and the light chain that remain covalently linked by a disulfide bond, domains structure overview Homo sapiens
50000
-
1 * 50000 + 1 * 38000, SDS-PAGE, the enzyme is proteolytically processed into the heavy and the light chain that remain covalently linked by a disulfide bond, domains structure overview Homo sapiens
66000
-
nonglycosylated proenzyme Homo sapiens
88000
-
mature enzyme Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein factor I is a multidomain acute phase glycoprotein, that is N-glycosylated at six positions (25-27%, w/w) with heavily sialylated biantennary glycans. Three-dimensional overview of the glycosylation sites. Deglycosylation by endoglycosidases, profile overview Homo sapiens

Source Tissue

Source Tissue Comment Organism Textmining
blood the enzyme circulates in a zymogen-like state in blood Homo sapiens
-
additional information the enzyme is produced mainly in the liver but also by monocytes, fibroblasts, keratinocytes, and endothelial cells Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Boc-Asp(benzyl)-Pro-Arg-4-methylcoumarin 7-amide + H2O
-
Homo sapiens ?
-
?

Subunits

Subunits Comment Organism
dimer 1 * 50000 + 1 * 38000, SDS-PAGE, the enzyme is proteolytically processed into the heavy and the light chain that remain covalently linked by a disulfide bond, domains structure overview Homo sapiens

Synonyms

Synonyms Comment Organism
factor I
-
Homo sapiens

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Homo sapiens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.4
-
assay at Homo sapiens

General Information

General Information Comment Organism
physiological function factor I is a serine protease that inhibits all complement pathways by degrading activated complement components C3b and C4b. It functions only in the presence of several cofactors, such as factor H, C4b-binding protein, complement receptor 1, and membrane cofactor protein Homo sapiens