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Literature summary for 3.4.21.38 extracted from

  • Fujikawa, K.; Kurachi, K.; Davie, E.W.
    Characterization of bovine factor XIIa (activated Hageman factor) (1977), Biochemistry, 16, 4182-4188.
    View publication on PubMed
Search for more literature for 3.4.21.38

Activating Compound

Activating Compound Comment Organism Structure
kaolin required for maximal activity Bos taurus

Inhibitors

Inhibitors Comment Organism Structure
antithrombin III inhibition is accelerated 300fold to 500fold by the addition of heparin, heparin alone has no effect; inhibitor is bound to the light chain of the enzyme which contains the active-site Ser residue Bos taurus
diisopropyl phosphofluoridate inhibitor is bound to the light chain of the enzyme which contains the active-site Ser residue Bos taurus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
31000
-
 1 * 31000 + 1 * 52000, SDS-PAGE Bos taurus
52000
-
 1 * 31000 + 1 * 52000, SDS-PAGE Bos taurus
74000
-
 sedimentation equilibrium centrifugation Bos taurus

Organism

Organism UniProt Comment Textmining
Bos taurus
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification the conversion of factor XII to factor XIIa is due to the cleavage of a specific internal Arg-Val peptide bond Bos taurus

Source Tissue

Source Tissue Comment Organism Textmining
blood plasma
-
 Bos taurus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
N-benzoyl-L-Phe-L-Val-L-Arg-4-nitroanilide + H2O
-
 Bos taurus ?
-
 ?
tosyl arginine methyl ester + H2O
-
 Bos taurus tosyl-Arg + methanol
-
 ?

Subunits

Subunits Comment Organism
dimer 1 * 31000 + 1 * 52000, SDS-PAGE Bos taurus