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• W2077726663 startingPage "30414" @default.
• W2077726663 abstract "Thrombin is produced by the ordered action of prothrombinase on two cleavage sites in prothrombin. Meizothrombin, a proteinase precursor of thrombin, is a singly cleaved species that accumulates abundantly as an intermediate. We now show that covalent linkage of the N-terminal propiece with the proteinase domain in meizothrombin imbues it with exceptionally zymogen-like character. Meizothrombin exists in a slowly reversible equilibrium between two equally populated states, differing by as much as 140-fold in their affinity for active site-directed ligands. The distribution between the two forms, designated zymogen-like and proteinase-like, is affected by Na(+), thrombomodulin binding, or active site ligation. In rapid kinetic measurements with prothrombinase, we also show that the zymogen-like form is produced following the initial cleavage reaction and slowly equilibrates with the proteinase-like form in a previously unanticipated rate-limiting step before it can be further cleaved to thrombin. The reversible equilibration of meizothrombin between zymogen- and proteinase-like states provides new insights into its ability to selectively exhibit the anticoagulant function of thrombin and the mechanistic basis for its accumulation during prothrombin activation. Our findings also provide unexpected insights into the regulation of proteinase function and how the formation of meizothrombin may yield a long lived intermediate with an important regulatory role in coagulation." @default.
• W2077726663 created "2016-06-24" @default.
• W2077726663 creator A5036209779 @default.
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• W2077726663 date "2012-08-01" @default.
• W2077726663 modified "2023-09-27" @default.
• W2077726663 title "Meizothrombin Is an Unexpectedly Zymogen-like Variant of Thrombin" @default.
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• W2077726663 doi "https://doi.org/10.1074/jbc.m112.394809" @default.
• W2077726663 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3436291" @default.
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