Information on EC 3.4.24.B39 - metallo-alpha-fibrinogenase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.4.24.B39
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
metallo-alpha-fibrinogenase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
The enzymes cleaves the Aalpha-chain of fibrinogen with high specificity
show the reaction diagram
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
azocasein + H2O
?
show the reaction diagram
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-
-
-
?
Bovine fibrinogen + H2O
?
show the reaction diagram
the enzyme rapidly hydrolyzes the Aalpha-chain of fibrinogen, followed by the Bbeta-chain and does not cleave the gamma-chain
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-
?
casein + H2O
?
show the reaction diagram
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-
-
-
?
D-Pro-Phe-Arg-4-nitroanilide + H2O
D-Pro-Phe-Arg + 4-nitroaniline
show the reaction diagram
-
synthetic substrate P7959
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-
?
Fibrin + H2O
?
show the reaction diagram
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-
-
-
?
Fibrinogen + H2O
?
show the reaction diagram
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the enzyme preferentially cleaves the Aalpha-chain of fibrinogen, followed by the Bbeta-chain and finally the gamma chain
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?
Fibronectin + H2O
?
show the reaction diagram
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-
-
-
?
Human fibrinogen + H2O
?
show the reaction diagram
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the enzyme cleaves dose-dependently the Aalpha-chain of human fibrinogen only. The enzyme cleaves a peptide with molecular weight of around 10 kDa from the C-terminus
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?
N-(4-tosyl)-Gly-Pro-Lys-4-nitroanilide + H2O
N-(4-tosyl)-Gly-Pro-Lys + 4-nitroaniline
show the reaction diagram
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best synthetic substrate, T6140
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-
?
N-benzoyl-Pro-Phe-Arg-4-nitroanilide + H2O
N-benzoyl-Pro-Phe-Arg + 4-nitroaniline
show the reaction diagram
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synthetic substrate B2133
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-
?
Oxidized insulin B-chain + H2O
?
show the reaction diagram
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the enzyme preferentially cleaves oxidized insulin B-chain at the site of Val12-Glu13, Leu15-Tyr16, and Phe24-Phe25
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-
?
plasmin + H2O
?
show the reaction diagram
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-
-
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?
type IV collagen
?
show the reaction diagram
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-
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?
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
Bovine fibrinogen + H2O
?
show the reaction diagram
A2TK72
the enzyme rapidly hydrolyzes the Aalpha-chain of fibrinogen, followed by the Bbeta-chain and does not cleave the gamma-chain
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?
Fibrin + H2O
?
show the reaction diagram
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?
Fibrinogen + H2O
?
show the reaction diagram
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the enzyme preferentially cleaves the Aalpha-chain of fibrinogen, followed by the Bbeta-chain and finally the gamma chain
-
-
?
Fibronectin + H2O
?
show the reaction diagram
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-
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?
Human fibrinogen + H2O
?
show the reaction diagram
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the enzyme cleaves dose-dependently the Aalpha-chain of human fibrinogen only. The enzyme cleaves a peptide with molecular weight of around 10 kDa from the C-terminus
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?
Oxidized insulin B-chain + H2O
?
show the reaction diagram
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the enzyme preferentially cleaves oxidized insulin B-chain at the site of Val12-Glu13, Leu15-Tyr16, and Phe24-Phe25
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?
plasmin + H2O
?
show the reaction diagram
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?
type IV collagen
?
show the reaction diagram
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?
additional information
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
benzamidine
complete inhibition at 1 mM
Cu2+
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83.8% residual activity at 3.2 mM
dithiothreitol
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incubation with 5 mM dithiothreitol results in 34% inhibition of azocasein hydrolysis
phenylmethylsulfonyl fluoride
tris-(2-carboxyethyl)phosphine hydrochloride
complete inhibition at 1 mM
Zn2+
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85.1% residual activity at 3.2 mM
additional information
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.5382
N-(4-tosyl)-Gly-Pro-Lys-4-nitroanilide
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at pH 8.0 and 37°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.419
N-(4-tosyl)-Gly-Pro-Lys-4-nitroanilide
Deinagkistrodon acutus
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at pH 8.0 and 37°C
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 8
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7 - 10.5
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the enzyme shows highest activity between pH 7.0 and 10.5. Activity drops sharply under more alkaline or acidic conditions with a complete loss of activity occurring at pH values 4.0 and 11.5
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 40
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30 - 50
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the enzyme shows highest activity between 30 and 50°C. Activity drops sharply under higher temperatures, with a complete loss of activity occurring above 60°C
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6
isoelectric focusing
9
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isoelectric focusing
10
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isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25000
x * 25000, SDS-PAGE
60000
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x * 60000, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60
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heating for 15 min at 60°C leads to an activity loss of 80-85%
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DEAE-Sephadex A-50 gel filtration and CM-Sephadex C-50 gel filtration
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
the enzyme has a clinical application for the therapy of thrombosis disease