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Literature summary for 3.4.21.74 extracted from

  • He, Q.; Li, H.; Zhou, B.; Wen, H.; Li, J.; Xiao, B.; Zhang, K.; Hodgson, W.C.; Yu, X.
    TA-2, a thrombin-like enzyme from the Chinese white-lipped green pitviper (Trimeresurus albolabris): isolation, biochemical and biological characterization (2012), Blood Coagul. Fibrinolysis, 23, 445-453.
    View publication on PubMed

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
Trimeresurus albolabris
-
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
38800
-
native PAGE Trimeresurus albolabris
47900
-
1 * 47900, SDS-PAGE Trimeresurus albolabris

Organism

Organism UniProt Comment Textmining
Trimeresurus albolabris
-
from China
-

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein the enzyme contains about 6% sugar Trimeresurus albolabris

Purification (Commentary)

Purification (Comment) Organism
native enzyme 12.7fold from venom to homogeneity by gel filtration, anion exchange and heparin affinity chromatography Trimeresurus albolabris

Source Tissue

Source Tissue Comment Organism Textmining
venom
-
Trimeresurus albolabris
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
108.6
-
purified native enzyme, pH 7.4, 37°C, substrate bovine fibrinogen Trimeresurus albolabris
192.3
-
purified native enzyme, pH 7.4, 37°C, substrate casein Trimeresurus albolabris

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Bovine fibrinogen + H2O coagulation Trimeresurus albolabris ?
-
?
casein + H2O high activity Trimeresurus albolabris ?
-
?
fibrinogen-releasing peptide A + H2O the enzyme cleaves the Aalpha- and the Bbeta-chains of fibrinogen-releasing peptides A and B Trimeresurus albolabris ?
-
?
fibrinogen-releasing peptide B + H2O the enzyme cleaves the Aalpha- and the Bbeta-chains of fibrinogen-releasing peptides A and B Trimeresurus albolabris ?
-
?
additional information no activity with fibrin, but high esterase activity with Nalpha-4-tosyl-L-arginine methyl ester Trimeresurus albolabris ?
-
?

Subunits

Subunits Comment Organism
monomer 1 * 47900, SDS-PAGE Trimeresurus albolabris
More the N-terminal sequenceis VVGGDECNIN Trimeresurus albolabris

Synonyms

Synonyms Comment Organism
TA-2
-
Trimeresurus albolabris
Thrombin-like enzyme
-
Trimeresurus albolabris
TLE
-
Trimeresurus albolabris

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Trimeresurus albolabris

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.4
-
assay at Trimeresurus albolabris

pI Value

Organism Comment pI Value Maximum pI Value
Trimeresurus albolabris isoelectric focusing
-
3.9

General Information

General Information Comment Organism
physiological function the enzyme acts as a promoter for platelet aggregation induced by ADP or collagen. It causes prolongation of bleeding in mice, but has no hemorrhagic and edema-inducing activities even at high concentrations Trimeresurus albolabris