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Literature summary for 3.4.21.22 extracted from

  • Gale, A.J.; Radtke, K.P.; Cunningham, M.A.; Chamberlain, D.; Pellequer, J.L.; Griffin, J.H.
    Intrinsic stability and functional properties of disulfide bond-stabilized coagulation factor VIIIa variants (2006), J. Thromb. Haemost., 4, 1315-1322.
    View publication on PubMed
Search for more literature for 3.4.21.22

Activating Compound

Activating Compound Comment Organism Structure
Factor VIIIa binding curves of FIXa and FVIIIa, binding of factor VIIIa with engineered disulfide bond resulting in a more stable FVIIIa: C662–C1828 FVIIIa binds with similar affinity to that of wild-type FVIIIa, while C664-C1826 FVIIIa binds to FIXa with a significantly lower affinity, binding structures, overview Homo sapiens
Phospholipids the vesicles binding the enzyme consist of 40% phosphatidylcholine, 20% phosphatidylserine, and 40% phosphatidylethanolamine Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
 Homo sapiens
-
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
factor X + H2O Homo sapiens
-
 activated factor X + ?
-
 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
commercial preparation from plasma Homo sapiens
-
plasma
-
 Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
factor X + H2O
-
 Homo sapiens activated factor X + ?
-
 ?
factor X + H2O proteolytic activity, factor IXa acts as part of the FXase complex with factor VIIIa on the surface of phospholipid vesicles, overview Homo sapiens activated factor X + ?
-
 ?