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The conversion of zymogen Factor X (FX) to an active protease involves the removal of a 52‐residue long activation peptide (AP). Through site‐directed mutagenesis, we investigate the role of the AP and demonstrate that the high abundance of proline residues is important for efficient proteolysis of FX. Moreover, we identify an essential interaction site for Factor IXa (FIXa) between residues 22 and...
Background
The regulation of factor X (FX) is critical to maintain the balance between blood coagulation and fluidity.
Objectives
To functionally characterize the role of the FX autolysis loop in the regulation of the zymogen and active form of FX.
Methods
We introduced novel N‐linked glycosylations on the surface‐exposed loop spanning residues 143–150 (chymotrypsin numbering) of FX. The activity...
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