EC Number   |
Posttranslational Modification |
Reference |
|---|
   3.4.21.7 | glycoprotein |
the human plasminogen is partially N-glycosylated at Asn289 and O-glycosylated at Ser249 and Thr346 giving rise to plasminogen variants I (Asn289, Thr346) and II (only Thr346) |
717469 |
| 3.4.21.7 | phosphoprotein |
plasminogen is partially phosphorylated at Ser578 |
717469 |
| 3.4.21.7 | proteolytic modification |
activation of plasminogen by cleavage of a sensitive Arg-Val peptide bond in the COOH-terminal portion of Glu-plasminogen to give the two-chain plasmin molecule, followed by the cleavage of a Lys-Lys peptide bond in the NH2-terminal portion of the molecule. The latter event results in the release of a peptide, or peptides |
95548 |
| 3.4.21.7 | proteolytic modification |
activation through cleavage by urokinase-type plasminogen activator is stimulated by the bacterial protease m3/6 from Pseudomonas fluorescens |
669645 |
| 3.4.21.7 | proteolytic modification |
cleavage of plasminogen to active plasmin by urokinase-type plasminogen activator, complex dynamics and mathematical modeling, overview |
717386 |
| 3.4.21.7 | proteolytic modification |
during activation of plasminogen, a peptide of 8200 Da is released from the plasminogen amino terminus |
95549 |
| 3.4.21.7 | proteolytic modification |
Glu-plasminogen is cleaved to plasmin for activation by thrombin, as well as by constitutively expressed tPA, i.e. tissue-type plasminogen activator, or uPA, i.e. urokinase-type plasminogen activator |
717216 |
| 3.4.21.7 | proteolytic modification |
mechanism of activation by urokinase, streptokinase, trypsin and pig heart activator is specific and proceeds primarily through the cleavage of a single Arg-Val bond |
95552 |
| 3.4.21.7 | proteolytic modification |
the main physiological activators of plasminogen are tissue-type plasminogen activator, which is mainly involved in the dissolution of the fibrin polymers by plasmin, and urokinase-type plasminogen activator, which is primarily responsible for the generation of plasmin activity in the intercellular space. Both activators are multidomain serine proteases. Pgn is activated by the two main physiological plasminogen activators to the active, two-chain plasmin molecule held together by two interchain disulfide bridges, Cys548-Cys666, Cys558-Cys566, by cleavage of the Arg561-Val562 peptide bond and the release of the 77-residue N-terminal peptide. Two N-terminally different forms of plasminogen exist, Glu-Pgn and Lys-Pgn. Lys-Pgn is formed by cleavage of the Lys77-Lys78 peptide bond in Glu-Pgn, releasing the N-terminal peptide |
717469 |
| 3.4.21.7 | proteolytic modification |
urokinase-type plasminogen activator cleaves plasminogen to give active plasmin |
-, 717845 |
