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Thrombin a-chain: activation remnant or allosteric effector?


ABSTRACT: 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.

SUBMITTER: Carter IS 

PROVIDER: S-EPMC3211113 | biostudies-literature | 2010

REPOSITORIES: biostudies-literature

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Thrombin a-chain: activation remnant or allosteric effector?

Carter Isis S R IS   Vanden Hoek Amanda L AL   Pryzdial Edward L G EL   Macgillivray Ross T A RT  

Thrombosis 20101209


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 remnan  ...[more]

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