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Biochemistry of factor X

M Hertzberg1

  • 1Department of Haematology, Westmead Hospital, NSW Australia.

Blood Reviews
|March 1, 1994
PubMed
Summary
This summary is machine-generated.

Factor X is a serine protease crucial for blood coagulation, forming complexes to convert prothrombin to thrombin. Its gene shares features with other vitamin K-dependent proteins, indicating common evolutionary origins and modular gene structure.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Hematology

Background:

  • Factor X is a key serine protease in the coagulation cascade.
  • It converges intrinsic and extrinsic pathways to form the active factor Xa.
  • Factor Xa, with cofactor Va, phospholipids, and calcium, converts prothrombin to thrombin.

Purpose of the Study:

  • To explore the structural and evolutionary relationships of the Factor X gene.
  • To understand the functional significance of modular domains within Factor X.
  • To investigate structure-function relationships using recombinant proteins and fragments.

Main Methods:

  • Comparative gene analysis of Factor X with other vitamin K-dependent proteins.
  • Analysis of protein domains encoded by exons.

Related Experiment Videos

  • Studies utilizing recombinant proteins and proteolytic fragments.

    • Main Results:

    • Factor X gene shares structural and organizational features with other vitamin K-dependent coagulation proteins.
    • Exons encode homologous domains responsible for specific functions.
    • Domains mediate gamma-carboxylase recognition, calcium binding, and surface interactions.

    Conclusions:

    • Factor X and related proteins likely evolved from a common ancestral gene.
    • The modular structure of Factor X contributes to its diverse functional properties.
    • Structure-function studies provide insights into protein module roles in coagulation.