EC Number   |
Posttranslational Modification |
Reference |
|---|
   3.4.21.73 | proteolytic modification |
activation of enzyme zymogen. Group A Streptococci are able to mediate a significant increase in the activation of zymogen pro-enzyme in human plasma. The zymogen pro-uPA can be activated by a variety of proteases, including plasmin |
732801 |
| 3.4.21.73 | proteolytic modification |
activation of human pro-urokinase by unrelated proteases secreted by Pseudomonas aeruginosa, e.g. LasB, a thermolysin-like metalloprotease, or protease IV, overview. Activation of pro-urokinase by purified LasB, or by the secretomes of Pseudomonas aeruginosa LasB-expressing or LasB-deficient strains |
717213 |
| 3.4.21.73 | proteolytic modification |
in the 2-chain urokinase, after cleavage of the single-chain proform, the polypeptide chains A and B, light and heavy chains, respectively, are connected by the Cys148-Cys279 disulfide bond. Thrombin hydrolysis provides the mechanism of proteolytic inactivation of uPA cleavage of the Arg156-Phe157 enzyme bond that does not exclude nonproteolytic functioning of such peptide forms |
707951 |
| 3.4.21.73 | proteolytic modification |
secretion in inactive forms, and activation by plasmin through proteolytic cleavage, mathematical modeling, overview |
717386 |
| 3.4.21.73 | proteolytic modification |
single-chain enzyme is converted to the two-chain form by incubation with immobilized plasmin, it can also be cleaved by plasmin at Lys158-Ile159 to produce potent two-chain enzyme accompanied by a conformational change in protein |
732184 |
| 3.4.21.73 | proteolytic modification |
single-chain uPA is cleaved to the activated two-chain form |
709091 |
| 3.4.21.73 | proteolytic modification |
the enzyme is initially synthesized as single-chain proenzyme with an activity that is many orders of magnitude lower than those of the mature enzyme. Proteolytic cleavage of an exposed loop liberates a new amino terminus that inserts into a hydrophobic pocket and forms a stabilizing salt bridge with a ubiquitously conserved aspartate residue, resulting in a conformational change organizing the mature oxyanion hole |
707518 |
| 3.4.21.73 | proteolytic modification |
the enzyme is produced as inactive pro-enzyme, which undergoes several post-translational modifications, the zymogen binds its own receptor uPAR and is cleaved by neighboring, membrane-bound plasmin or other proteases at K158-K159 to produce the active two-chain form held together by a single disulfide bond, further cleavage of pro-uPA at K135-K136 releases the amino-terminal fragment of uPA, overview |
683550 |
| 3.4.21.73 | proteolytic modification |
the enzyme is synthesized intracellularly as a single chain, inactive proenzyme, is secreted, binds to its receptor and is activated more than 30fold |
731429 |
| 3.4.21.73 | proteolytic modification |
the zymogen form pro-uPA is cleaved to the active two-chain uPA |
717222 |
