Factor Xa: Difference between revisions
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===Activation peptide=== | ===Activation peptide=== | ||
Chymotrypsin-like proteases are synthesized as inactive precursors (“zymogens”) containing N-terminal extensions. Four segments are deformed in the zymogens of chymotrypsin and trypsin: the N-terminus to residue 19, residues 142-152, 184-193, and 216- 223 (these regions are collectively termed the activation domain36). This deformed region includes the S1 site and oxyanion hole, which explains the low activity of the zymogen. Proteolytic processing activates the zymogen, releasing the N-terminal Ile16. The new N-terminus forms a buried salt bridge with Asp194, inducing a conformational change that orders the activation domain. The S1 site and oxyanion hole are formed, creating the active protease. | Chymotrypsin-like proteases are synthesized as inactive precursors (“zymogens”) containing N-terminal extensions. Four segments are deformed in the zymogens of chymotrypsin and trypsin: the N-terminus to residue 19, residues 142-152, 184-193, and 216- 223 (these regions are collectively termed the activation domain36). This deformed region includes the S1 site and oxyanion hole, which explains the low activity of the zymogen. Proteolytic processing activates the zymogen, releasing the N-terminal Ile16. The new N-terminus forms a buried salt bridge with Asp194, inducing a conformational change that orders the activation domain. The S1 site and oxyanion hole are formed, creating the active protease. | ||
==Post-Translational Modifications== | |||
human factor X had four carbohydrate-attachment sites, namely, O-glycosidic linkages to Thr17 and Thr29, respectively, and N-glycosidic linkages to Asn39 and Asn49, respectively, in their activation peptides | |||
==Enzyme Mechanism== | ==Enzyme Mechanism== | ||
