Information on EC 3.4.21.85 - limulus clotting factor B

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The expected taxonomic range for this enzyme is: Tachypleus tridentatus

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EC NUMBER
COMMENTARY hide
3.4.21.85
-
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RECOMMENDED NAME
GeneOntology No.
limulus clotting factor B
-
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
Selective cleavage of -Arg98-/-Ile- bond in limulus proclotting enzyme to form active clotting enzyme
show the reaction diagram
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-
-
-
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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
848851-53-6
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
Benzoyl-Ser-Ser-Arg 4-methylcoumarin 7-amide + H2O
?
show the reaction diagram
-
-
-
-
-
Benzoyl-Ser-Thr-Arg 4-methylcoumarin 7-amide + H2O
?
show the reaction diagram
-
-
-
-
-
Benzoyl-Thr-Ser-Arg 4-methylcoumarin 7-amide + H2O
?
show the reaction diagram
-
-
-
-
-
Benzoyl-Thr-Thr-Arg 4-methylcoumarin 7-amide + H2O
?
show the reaction diagram
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-
-
-
-
Limulus proclotting enzyme + H2O
Active clotting enzyme
show the reaction diagram
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-
-
-
-
N-tert-Butoxycarbonyl-Met-Thr-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-Arg-Arg 4-methylcoumarin 7-amide + H2O
?
show the reaction diagram
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-
-
-
-
Tert-Butoxycarbonyl-Leu-Thr-Arg 4-methylcoumarin 7-amide + H2O
?
show the reaction diagram
-
-
-
-
-
Tert-Butoxycarbonyl-Val-Pro-Arg-4-methylcoumaryl-7-amide + H2O
?
show the reaction diagram
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-
-
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additional information
?
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3 protease zymogens, factor C, factor B, and proclotting enzyme are required for the sequential activation of the limulus clotting system. Factor B is activated by factor C (sensitive to lipopolysaccharide) and the resulting factor B activates proclotting enzyme to the clotting enzyme
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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
additional information
?
-
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3 protease zymogens, factor C, factor B, and proclotting enzyme are required for the sequential activation of the limulus clotting system. Factor B is activated by factor C (sensitive to lipopolysaccharide) and the resulting factor B activates proclotting enzyme to the clotting enzyme
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
alpha2-Plasmin inhibitor
-
-
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benzamidine
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
factor B is activated by Limulus clotting factor C
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25000
-
1 * 32000 + 1 * 25000, Tachypleus tridentatus, SDS-PAGE under reducing conditions, 1 * 56000, Tachypleus tridentatus, SDS-PAGE under nonreducing conditions; factor B (zymogen) is a mixture of single-chain and two-chain forms: x * 64000, Tachypleus tridentatus, SDS-PAGE without 2-mercaptoethanol, x * 64000 + x * 40000 + x * 25000, Tachypleus tridentatus, SDS-PAGE after reduction with 2-mercaptoethanol
32000
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1 * 32000 + 1 * 25000, Tachypleus tridentatus, SDS-PAGE under reducing conditions, 1 * 56000, Tachypleus tridentatus, SDS-PAGE under nonreducing conditions
40000
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factor B (zymogen) is a mixture of single-chain and two-chain forms: x * 64000, Tachypleus tridentatus, SDS-PAGE without 2-mercaptoethanol, x * 64000 + x * 40000 + x * 25000, Tachypleus tridentatus, SDS-PAGE after reduction with 2-mercaptoethanol
40570
-
x * 40570, calculated
56000
-
1 * 32000 + 1 * 25000, Tachypleus tridentatus, SDS-PAGE under reducing conditions, 1 * 56000, Tachypleus tridentatus, SDS-PAGE under nonreducing conditions
64000
-
factor B (zymogen) is a mixture of single-chain and two-chain forms: x * 64000, Tachypleus tridentatus, SDS-PAGE without 2-mercaptoethanol, x * 64000 + x * 40000 + x * 25000, Tachypleus tridentatus, SDS-PAGE after reduction with 2-mercaptoethanol
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 40570, calculated
dimer
-
1 * 32000 + 1 * 25000, Tachypleus tridentatus, SDS-PAGE under reducing conditions, 1 * 56000, Tachypleus tridentatus, SDS-PAGE under nonreducing conditions
additional information
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
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sequence contains a prepropeptide of 23 amino acids, that may be processed by both a signal peptidase and a processing protease. Cleavage sites of the zymogen for activation by limulus active factor C are an Arg-Ser and an Ile-Ile bond
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 9
-
24 h, stable, factor B zymogen
29793
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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LINKS TO OTHER DATABASES (specific for EC-Number 3.4.21.85)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)