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J Thromb Haemost. 2009 Jul;7 Suppl 1:159-64. doi: 10.1111/j.1538-7836.2009.03365.x.

Slow thrombin is zymogen-like.

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1
Department of Haematology, Cambridge Institute for Medical Research, University of Cambridge, Cambridge, UK. jah52@cam.ac.uk

Abstract

Blood coagulation is the result of a cascade of zymogen activation events; however, its initiation is allosteric. Factor VIIa circulates in a zymogen-like state and is allosterically activated by binding to tissue factor. Thrombin, the final protease generated in the blood coagulation cascade, has also been shown to exist in a low activity state in the absence of cofactors, and the structural features of this 'slow' form have been studied for many years. In this manuscript, I will review the general features that render zymogens inactive and how proteolytic cleavage results in activation, but I will also show how this distinction is blurred by zymogens that have activity (protease-like zymogens) and proteases with low activity (zymogen-like proteases). This will then be applied in the analysis of slow thrombin to reveal how allosteric activation of thrombin simply reflects the conversion from a zymogen-like enzyme to an active serine protease.

PMID:
19630791
PMCID:
PMC2717038
DOI:
10.1111/j.1538-7836.2009.03365.x
[Indexed for MEDLINE]
Free PMC Article
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