Factor V: a prototype pro-cofactor for vitamin K-dependent enzyme complexes in blood clotting.
The relative abundance of factor V, factor X and prothrombin has enabled detailed analyses of the prothrombinase complex. Determination of the primary structure for factor V has provided the basis for examination of structure-function relationships. The imminent in vitro expression of recombinant factor V will provide the opportunity for site-specific mutagenesis and a verification of these structure-function relationships. A comparison of the physical properties and primary structures for factors V and VIII has revealed extensive similarities in these two cofactor proteins. This observation indicates that a direct application of the technology developed for the analysis of prothrombinase will lead to an equal understanding of the factor Xase complex. Whether similar relationships exist for other blood coagulation enzyme complexes remains to be determined.
Jenny
R J
RJ
Mann
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KG
D005165:Factor V / Q000096:biosynthesis / Q000378:metabolism* / Q000502:physiology*; D005169:Factor VIII; D015943:Factor Va / Q000378:metabolism; D005170:Factor X / Q000378:metabolism*; D015951:Factor Xa; D006801:Humans; D015394:Molecular Structure
C022475:prothrombinase complex; D015943:Factor Va; D005165:Factor V; D005169:Factor VIII; D005170:Factor X; D015951:Factor Xa