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Literature summary for 3.4.24.B39 extracted from

  • 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 (2014), Protein Expr. Purif., 99, 99-105.
    View publication on PubMed

Application

Application Comment Organism
medicine the enzyme has a clinical application for the therapy of thrombosis disease Deinagkistrodon acutus

Inhibitors

Inhibitors Comment Organism Structure
benzamidine complete inhibition at 1 mM Deinagkistrodon acutus
additional information not inhibited by EDTA Deinagkistrodon acutus
phenylmethylsulfonyl fluoride complete inhibition at 1 mM Deinagkistrodon acutus
tris-(2-carboxyethyl)phosphine hydrochloride complete inhibition at 1 mM Deinagkistrodon acutus

Metals/Ions

Metals/Ions Comment Organism Structure
additional information no Zn2+, Ca2+, Ni2+, Co2+ and Cu2+ are detected in the purified enzyme Deinagkistrodon acutus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
25000
-
x * 25000, SDS-PAGE Deinagkistrodon acutus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
Bovine fibrinogen + H2O Deinagkistrodon acutus the enzyme rapidly hydrolyzes the Aalpha-chain of fibrinogen, followed by the Bbeta-chain and does not cleave the gamma-chain ?
-
?
additional information Deinagkistrodon acutus the enzyme is devoid of fibrinolytic activity and also exhibits arginine esterase activity ?
-
?

Organism

Organism UniProt Comment Textmining
Deinagkistrodon acutus A2TK72
-
-

Purification (Commentary)

Purification (Comment) Organism
DEAE-Sephadex A-50 gel filtration and CM-Sephadex C-50 gel filtration Deinagkistrodon acutus

Source Tissue

Source Tissue Comment Organism Textmining
venom
-
Deinagkistrodon acutus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Bovine fibrinogen + H2O the enzyme rapidly hydrolyzes the Aalpha-chain of fibrinogen, followed by the Bbeta-chain and does not cleave the gamma-chain Deinagkistrodon acutus ?
-
?
additional information the enzyme is devoid of fibrinolytic activity and also exhibits arginine esterase activity Deinagkistrodon acutus ?
-
?

Subunits

Subunits Comment Organism
? x * 25000, SDS-PAGE Deinagkistrodon acutus

Synonyms

Synonyms Comment Organism
alpha-Fibrinogenase
-
Deinagkistrodon acutus
DAnase
-
Deinagkistrodon acutus

pI Value

Organism Comment pI Value Maximum pI Value
Deinagkistrodon acutus isoelectric focusing
-
6

General Information

General Information Comment Organism
physiological function the enzyme's fibrinogenolytic activity is involved in its inhibition of ADP-induced platelet aggregation Deinagkistrodon acutus