Information on EC 3.4.21.84 - limulus clotting factor C

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.4.21.84
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RECOMMENDED NAME
GeneOntology No.
limulus clotting factor C
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
Selective cleavage of -Arg103-/-Ser- and -Ile124-/-Ile- bonds in limulus clotting factor B to form factor _overbar_B_. Cleavage of -Pro-Arg-/- bonds in synthetic substrates
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
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-
-
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CAS REGISTRY NUMBER
COMMENTARY hide
115743-27-6
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
horseshoe crab
UniProt
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
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RNAi silencing results in a significant reduction in phagocytic activity of tick hemocytes against the Gram-negative bacteria Chryseobacterium indologenes and Escherichia coli, but not against the yeast, Candida albicans
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
Limulus clotting factor B
Limulus clotting factor Bbar
show the reaction diagram
lipopolysaccharide + H2O
?
show the reaction diagram
binds a pathogen-associated LPS molecule to trigger a blood coagulation cascade
-
?
N-tert-Butoxycarbonyl-Asp(O-benzyl)-Pro-Arg 4-methylcoumarin 7-amide + H2O
?
show the reaction diagram
N-tert-Butoxycarbonyl-Leu-Gly-Arg 4-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
-
N-tert-Butoxycarbonyl-Thr-Ser-Arg 4-nitroanilide + H2O
?
show the reaction diagram
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-
-
-
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N-tert-Butoxycarbonyl-Val-Pro-Arg 4-nitroanilide + H2O
?
show the reaction diagram
tert-butoxycarbonyl-Asp(O-benzyl)-Ala-Arg 4-methylcoumarin 7-amide + H2O
?
show the reaction diagram
tert-butoxycarbonyl-Asp-Pro-Arg 4-methylcoumarin 7-amide + H2O
?
show the reaction diagram
tert-butoxycarbonyl-Gln-Pro-Arg 4-methylcoumarin 7-amide + H2O
?
show the reaction diagram
tert-butoxycarbonyl-Glu(O-benzyl)-Gly-Arg 4-methylcoumarin 7-amide + H2O
?
show the reaction diagram
tert-butoxycarbonyl-Gly-Ala-Arg-4-methylcoumarin 7-amide + H2O
?
show the reaction diagram
tert-butoxycarbonyl-Gly-Pro-Arg 4-methylcoumarin 7-amide + H2O
?
show the reaction diagram
tert-butoxycarbonyl-Ile-Gly-Arg 4-methylcoumarin 7-amide + H2O
?
show the reaction diagram
Tert-Butoxycarbonyl-Lys(benzyloxycarbonyl)-Gly-Arg-4-methylcoumarin 7-amide + H2O
?
show the reaction diagram
Tert-Butoxycarbonyl-Lys-Gly-Arg 4-methylcoumaryl 7-amide + H2O
?
show the reaction diagram
Tert-Butoxycarbonyl-Met-Ala-Arg 4-methylcoumarin 7-amide + H2O
?
show the reaction diagram
Tert-Butoxycarbonyl-Ser(O-benzyl)-Ala-Arg 4-methylcoumarin 7-amide + H2O
?
show the reaction diagram
Tert-Butoxycarbonyl-Val-Gly-Arg 4-methylcoumarin 7-amide + H2O
?
show the reaction diagram
Tert-Butoxycarbonyl-Val-Pro-Arg 4-methylcoumarin 7-amide + H2O
?
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
Limulus clotting factor B
Limulus clotting factor Bbar
show the reaction diagram
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active factor Cbar selectively cleaves the Arg103-/-Ser104 and Ile124-/-Ile125 bonds in proenzyme factor B to form factor Bbar, which then activates proclotting enzyme to clotting enzyme. The resulting clotting enzyme acts on coagulogen, causing the formation of an insoluble coagulin gel
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lipopolysaccharide + H2O
?
show the reaction diagram
Q26422
binds a pathogen-associated LPS molecule to trigger a blood coagulation cascade
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?
additional information
?
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
antithrombin III
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-
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benzamidine
D-Phe-Pro-Arg chloromethyl ketone
leupeptin
LICI-1
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the serpin specifically inhibits factor Cbar
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additional information
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no inhibition by alpha2-plasmin inhibitor
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.054
N-tert-Butoxycarbonyl-Val-Pro-Arg 4-nitroanilide
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0.19
tert-butoxycarbonyl-Ala-Pro-Arg 4-methylcoumarin 7-amide
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0.039
Tert-Butoxycarbonyl-Asp(O-benzyl)-Ala-Arg 4-methylcoumarin 7-amide
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0.026
tert-butoxycarbonyl-Asp(O-benzyl)-Pro-Arg 4-methylcoumarin 7-amide
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0.066
Tert-Butoxycarbonyl-Gln-Pro-Arg 4-methylcoumarin 7-amide
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0.045
tert-butoxycarbonyl-Lys(benzyloxycarbonyl)-Gly-Arg 4-methylcoumarin 7-amide
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0.088
Tert-Butoxycarbonyl-Met-Ala-Arg 4-methylcoumarin 7-amide
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0.114
Tert-Butoxycarbonyl-Val-Pro-Arg 4-methylcoumarin 7-amide
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additional information
additional information
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
391
N-tert-Butoxycarbonyl-Val-Pro-Arg 4-nitroanilide
Tachypleus tridentatus
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72
tert-butoxycarbonyl-Ala-Pro-Arg 4-methylcoumarin 7-amide
Tachypleus tridentatus
-
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18
Tert-Butoxycarbonyl-Asp(O-benzyl)-Ala-Arg 4-methylcoumarin 7-amide
Tachypleus tridentatus
-
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75
tert-butoxycarbonyl-Asp(O-benzyl)-Pro-Arg 4-methylcoumarin 7-amide
Tachypleus tridentatus
-
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34
Tert-Butoxycarbonyl-Gln-Pro-Arg 4-methylcoumarin 7-amide
Tachypleus tridentatus
-
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10
tert-butoxycarbonyl-Lys(benzyloxycarbonyl)-Gly-Arg 4-methylcoumarin 7-amide
Tachypleus tridentatus
-
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27
Tert-Butoxycarbonyl-Met-Ala-Arg 4-methylcoumarin 7-amide
Tachypleus tridentatus
-
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48
Tert-Butoxycarbonyl-Val-Pro-Arg 4-methylcoumarin 7-amide
Tachypleus tridentatus
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-
additional information
additional information
Tachypleus tridentatus
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
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enzyme mRNA is expressed in all stages including eggs
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
123000
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x * 123000, Limulus polyphemus, SDS-PAGE under nonreducing conditions
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
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the proenzyme Limulus coagulation factor C is autocatalytically converted to its active form, factor Cbar
additional information
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one enzyme molecule contains 24 residues of hexose and 31 residues of hexosamine
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
CrFC gene, in vitro studies in Drosophila sp. cell lines using factor C promoter-reporter chimera DNA constructs
of the zymogen factor C
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
mRNA levels were markedly increased upon injection of sterile saline or in response to injury
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
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recombinant factor C assay for measuring endotoxin in house dust: comparison with LAL, and (1->3)-beta-D-glucans. In the Limulus amebocyte lysate assay endotoxin is detected through a reaction cascade, initiated by the binding of endotoxins to Factor C. The advantage of an assay using the genetically engineered factor Cbar in measuring endotoxins is that recombinant factor Cbar does not contain factor G that can produce interference from (1->3)-beta-D-glucans