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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

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: C662Ā–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 + ?
-
?