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Information on EC 3.4.24.B39 - metallo-alpha-fibrinogenase and Organism(s) Deinagkistrodon acutus and UniProt Accession A2TK72

for references in articles please use BRENDA:EC3.4.24.B39
preliminary BRENDA-supplied EC number
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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.24 Metalloendopeptidases
                3.4.24.B39 metallo-alpha-fibrinogenase
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This record set is specific for:
Deinagkistrodon acutus
UNIPROT: A2TK72
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Word Map
The taxonomic range for the selected organisms is: Deinagkistrodon acutus
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
The enzymes cleaves the Aalpha-chain of fibrinogen with high specificity
Synonyms
danase, alpha-fg, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
alpha-Fibrinogenase
-
fibrinogenase
-
-
SUBSTRATE
PRODUCT                       
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
the enzyme rapidly hydrolyzes the Aalpha-chain of fibrinogen, followed by the Bbeta-chain and does not cleave the gamma-chain
-
-
?
azocasein + H2O
?
show the reaction diagram
-
-
-
-
?
casein + H2O
?
show the reaction diagram
-
-
-
-
?
D-Pro-Phe-Arg-4-nitroanilide + H2O
D-Pro-Phe-Arg + 4-nitroaniline
show the reaction diagram
-
synthetic substrate P7959
-
-
?
Fibrin + H2O
?
show the reaction diagram
-
-
-
-
?
Fibrinogen + H2O
?
show the reaction diagram
-
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
-
-
-
-
?
N-(4-tosyl)-Gly-Pro-Lys-4-nitroanilide + H2O
N-(4-tosyl)-Gly-Pro-Lys + 4-nitroaniline
show the reaction diagram
-
best synthetic substrate, T6140
-
-
?
N-benzoyl-Pro-Phe-Arg-4-nitroanilide + H2O
N-benzoyl-Pro-Phe-Arg + 4-nitroaniline
show the reaction diagram
-
synthetic substrate B2133
-
-
?
Oxidized insulin B-chain + H2O
?
show the reaction diagram
-
the enzyme preferentially cleaves oxidized insulin B-chain at the site of Val12-Glu13, Leu15-Tyr16, and Phe24-Phe25
-
-
?
plasmin + H2O
?
show the reaction diagram
-
-
-
-
?
type IV collagen
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
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
the enzyme rapidly hydrolyzes the Aalpha-chain of fibrinogen, followed by the Bbeta-chain and does not cleave the gamma-chain
-
-
?
Fibrin + H2O
?
show the reaction diagram
-
-
-
-
?
Fibrinogen + H2O
?
show the reaction diagram
-
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
-
-
-
-
?
Oxidized insulin B-chain + H2O
?
show the reaction diagram
-
the enzyme preferentially cleaves oxidized insulin B-chain at the site of Val12-Glu13, Leu15-Tyr16, and Phe24-Phe25
-
-
?
plasmin + H2O
?
show the reaction diagram
-
-
-
-
?
type IV collagen
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
benzamidine
complete inhibition at 1 mM
phenylmethylsulfonyl fluoride
complete inhibition at 1 mM
tris-(2-carboxyethyl)phosphine hydrochloride
complete inhibition at 1 mM
Cu2+
-
83.8% residual activity at 3.2 mM
dithiothreitol
-
incubation with 5 mM dithiothreitol results in 34% inhibition of azocasein hydrolysis
EDTA
-
29.6% residual activitty at 5 mM
phenylmethylsulfonyl fluoride
-
1.2% residual activitty at 2 mM
Zn2+
-
85.1% residual activity at 3.2 mM
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.5382
N-(4-tosyl)-Gly-Pro-Lys-4-nitroanilide
-
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
-
at pH 8.0 and 37°C
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 10.5
-
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
30 - 50
-
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
-
isoelectric focusing
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
the enzyme's fibrinogenolytic activity is involved in its inhibition of ADP-induced platelet aggregation
physiological function
-
the enzyme dose-dependently inhibits platelet aggregation triggered by ADP (0.005 mM) in human platelet-rich plasma. The enzyme cannot activate plasminogen
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
VM3A2_DEIAC
233
0
26713
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25000
x * 25000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 25000, SDS-PAGE
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
medicine
-
in an lipopolysaccharide-induced endotoxemia mice model, fibrinogenase treatment significantly increases the survival rate, remarkably protects liver and kidney from lipopolysaccharide damage as well as decreasing TNF-alpha level. In vitro, fibrinogenase significantly decreases LPS-induced TNF-alpha production and the expression of P-NF-kappaB
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Jiang, W.; Ma, T.; Su, X.; Qiu, P.; Yan, G.
Enzymatic activities and functional characterization of a novel recombinant snake venom proteinase from Agkistrodon acutus
Biochimie
91
277-287
2009
Deinagkistrodon acutus
Manually annotated by BRENDA team
Wang, S.; Xu, X.; Gao, S.; Zhu, S.; Rong, R.; Li, B.
Purification and partial characterization of a novel fibrinogenase from the venom of Deinagkistrodon acutus: inhibition of platelet aggregation
Protein Expr. Purif.
99
99-105
2014
Deinagkistrodon acutus (A2TK72), Deinagkistrodon acutus
Manually annotated by BRENDA team
Wang, Y.; Qin, Z.; Shen, S.; Xiang, N.; Liu, J.; Lin, X.; Bai, Z.; Wu, Z.
A novel fibrinogenase from Agkistrodon acutus venom protects against LPS-induced endotoxemia via regulating NF-?B pathway
Immunopharmacol. Immunotoxicol.
37
413-420
2015
Deinagkistrodon acutus
Manually annotated by BRENDA team