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Literature summary for 3.4.21.74 extracted from

  • Yu, X.; Li, Z.; Xia, X.; Fang, H.; Zhou, C.; Chen, H.
    Expression and purification of ancrod, an anticoagulant drug, in Pichia pastoris (2007), Protein Expr. Purif., 55, 257-261.
    View publication on PubMed

Application

Application Comment Organism
medicine high-level production of ancrod by Pichia pastoris has the potential to be used clinically Calloselasma rhodostoma

Cloned(Commentary)

Cloned (Comment) Organism
cDNA encoding ancrod synthesized with a yeast bias codon and inserted into the eukaryotic expression vector pPIC9, subsequently expressed in Pichia pastoris strain GS115 Calloselasma rhodostoma

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
additional information
-
broad 43000-48000 band, corresponding to the complex glycosylated ancrod, purified protein, zymography Calloselasma rhodostoma

Organism

Organism UniProt Comment Textmining
Calloselasma rhodostoma
-
-
-

Purification (Commentary)

Purification (Comment) Organism
by hydrophobic, affinity, and ion exchange chromatography Calloselasma rhodostoma

Source Tissue

Source Tissue Comment Organism Textmining
venom
-
Calloselasma rhodostoma
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
696
-
purified recombinant enzyme, specific fibrinogen clotting activity Calloselasma rhodostoma

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Fibrinogen + H2O recombinant ancrod coagulates fibrinogen by hydrolysis of the Aalpha chain similar to the native protein Calloselasma rhodostoma ?
-
?

Synonyms

Synonyms Comment Organism
Ancrod
-
Calloselasma rhodostoma