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Literature summary for 3.4.21.74 extracted from

  • Nolan, C.; Hall, L.S.; Barlow, G.H.
    Ancrod, the coagulating enzyme from Malayan pit viper (Agkistrodon rhodostoma) venom (1976), Methods Enzymol., 45, 205-213.
    View publication on PubMed
Search for more literature for 3.4.21.74

Inhibitors

Inhibitors Comment Organism Structure
4-Nitrophenyl-4-guanidinobenzoate
-
 Calloselasma rhodostoma
agmatine
-
 Calloselasma rhodostoma
Alpha-macroglobulin
-
 Calloselasma rhodostoma
alpha-N-(4-Nitrobenzyloxycarbonyl)-Arg chloromethyl ketone
-
 Calloselasma rhodostoma
antithrombin III
-
 Calloselasma rhodostoma
arginine
-
 Calloselasma rhodostoma
diisopropyl fluorophosphate
-
 Calloselasma rhodostoma
guanidinium ions
-
 Calloselasma rhodostoma
additional information no inhibition by Nalpha-p-tosyl-L-lysine chloromethyl ketone Calloselasma rhodostoma
PMSF
-
 Calloselasma rhodostoma

Localization

Localization Comment Organism GeneOntology No. Textmining
soluble
-
 Calloselasma rhodostoma
-
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
additional information
-
 amino acid composition Calloselasma rhodostoma
35400
-
 Agkistrodon rhodostoma, sedimentation equilibrium Calloselasma rhodostoma

Organism

Organism UniProt Comment Textmining
Calloselasma rhodostoma
-
 Malayan pit viper, formerly EC 3.4.21.28
-

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein high carbohydrate content Calloselasma rhodostoma

Purification (Commentary)

Purification (Comment) Organism
affinity chromatography, several forms, separable by electrophoresis and isoelectric focusing 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
33.7
-
 tosyl-L-Arg methyl ester Calloselasma rhodostoma

Storage Stability

Storage Stability Organism
5°C, pH 5-6.8, several months Calloselasma rhodostoma

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Fibrinogen + H2O splits fibrinopeptide A from Aalpha-chains by hydrolysis of Arg-Gly bond, but does not split this bond in Bbeta-chain Calloselasma rhodostoma ?
-
 ?
Fibrinogen + H2O or gamma-chain Calloselasma rhodostoma ?
-
 ?
additional information no activation of human factor VIII Calloselasma rhodostoma ?
-
 ?
additional information Ancrod has a high degree of specificity for Arg esters and peptide bonds involving carboxyl group of Arg residues Calloselasma rhodostoma ?
-
 ?
additional information no hydrolysis of native casein, denatured hemoglobin, Nalpha-benzoyl-Arg ethyl ester Calloselasma rhodostoma ?
-
 ?
Nalpha-Benzoyl-L-Arg cyclohexyl ester + H2O
-
 Calloselasma rhodostoma Nalpha-Benzoyl-L-Arg + cyclohexanol
-
 ?
Nalpha-Benzoyl-L-Arg ethyl ester + H2O
-
 Calloselasma rhodostoma Nalpha-Benzoyl-L-Arg + ethanol
-
 ?
Nalpha-Benzoyl-L-Arg methyl ester + H2O
-
 Calloselasma rhodostoma Nalpha-Benzoyl-L-Arg + methanol
-
 ?
Tosyl-L-arginine methyl ester + H2O
-
 Calloselasma rhodostoma Tosyl-L-arginine + methanol
-
 ?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Calloselasma rhodostoma

pH Stability

pH Stability pH Stability Maximum Comment Organism
5 6.8 several months stable at 5°C Calloselasma rhodostoma