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Literature summary 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

Activating Compound

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

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.21.38 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
3.4.21.38 diisopropyl phosphofluoridate inhibitor is bound to the light chain of the enzyme which contains the active-site Ser residue Bos taurus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.4.21.38 31000
-
 1 * 31000 + 1 * 52000, SDS-PAGE Bos taurus
3.4.21.38 52000
-
 1 * 31000 + 1 * 52000, SDS-PAGE Bos taurus
3.4.21.38 74000
-
 sedimentation equilibrium centrifugation Bos taurus

Organism

EC Number Organism UniProt Comment Textmining
3.4.21.38 Bos taurus
-
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.4.21.38 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

EC Number Source Tissue Comment Organism Textmining
3.4.21.38 blood plasma
-
 Bos taurus
-

Substrates and Products (Substrate)

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

Subunits

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