Table of Contents
Volume 2010, Article ID 416167, 9 pages
Review Article

Thrombin A-Chain: Activation Remnant or Allosteric Effector?

1Centre for Blood Research, University of British Columbia (UBC), Vancouver, BC, Canada V6T 1Z3
2Department of Biochemistry and Molecular Biology, (UBC), Vancouver, BC, Canada V6T 1Z3
3R and D Canadian Blood Services, Ottawa, ON, Canada K1G 4J5
4Department of Pathology and Laboratory Medicine, (UBC), Vancouver, BC, Canada V6T 1Z3

Received 26 August 2010; Accepted 27 October 2010

Academic Editor: Frank C. Church

Copyright © 2010 Isis S. R. Carter et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


Although prothrombin is one of the most widely studied enzymes in biology, the role of the thrombin A-chain has been neglected in comparison to the other domains. This paper summarizes the current data on the prothrombin catalytic domain A-chain region and the subsequent thrombin A-chain. Attention is given to biochemical characterization of naturally occurring prothrombin A-chain mutations and alanine scanning mutants in this region. While originally considered to be simply an activation remnant with little physiologic function, the thrombin A-chain is now thought to play a role as an allosteric effector in enzymatic reactions and may also be a structural scaffold to stabilize the protease domain.