EC Number   |
Reaction |
Reference |
|---|
   3.4.21.5 | selective cleavage of Arg-/-Gly bonds in fibrinogen to form fibrin and release fibrinopeptides A and B |
- |
- |
| 3.4.21.5 | selective cleavage of Arg-/-Gly bonds in fibrinogen to form fibrin and release fibrinopeptides A and B |
active site and P1' interactions, overview |
649116 |
| 3.4.21.5 | selective cleavage of Arg-/-Gly bonds in fibrinogen to form fibrin and release fibrinopeptides A and B |
Asp189 is involved in substrate recognition |
652512 |
| 3.4.21.5 | selective cleavage of Arg-/-Gly bonds in fibrinogen to form fibrin and release fibrinopeptides A and B |
catalytic tetrad, composed of His57, Asp102, Ser195, and Ser214, at the bottom of a canyon-like cleft shaping the catalytic pocket, further regulation of specificity by recognition domains along with insertion loops |
653060 |
| 3.4.21.5 | selective cleavage of Arg-/-Gly bonds in fibrinogen to form fibrin and release fibrinopeptides A and B |
mechanism, modeling |
650708 |
| 3.4.21.5 | selective cleavage of Arg-/-Gly bonds in fibrinogen to form fibrin and release fibrinopeptides A and B |
reaction mechanism, substrate binding, preference at positions P1-P4, molecular modeling of enzyme-substrate complex |
653290 |
| 3.4.21.5 | selective cleavage of Arg-/-Gly bonds in fibrinogen to form fibrin and release fibrinopeptides A and B |
serine protease |
652618 |
| 3.4.21.5 | selective cleavage of Arg-/-Gly bonds in fibrinogen to form fibrin and release fibrinopeptides A and B |
serine protease, for substrate binding P1 and P2 residues must be compatible with the geometry and chemistry of S1 and S2 specificity sites in thrombin, a glycine in P5 position is necessary for conserved substrate conformation, the hydrophobic residues, which occupy the aryl binding site of the enzyme determine the substrate conformation further away from the catalytic residues |
652062 |
| 3.4.21.5 | selective cleavage of Arg-/-Gly bonds in fibrinogen to form fibrin and release fibrinopeptides A and B |
serine protease, mechanism and substrate binding |
652864 |
| 3.4.21.5 | selective cleavage of Arg-/-Gly bonds in fibrinogen to form fibrin and release fibrinopeptides A and B |
two active site loops, residues 214-222 and residues 126-132, undergo decreases in solvent accessibility due to steric contacts with substrate. Two regions outside the active site undergo solvent protection upon substrate binding |
667605 |
