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Literature summary for 3.4.23.48 extracted from
- Fibrinolytic and procoagulant activities of Yersinia pestis and Salmonella enterica (2015), J. Thromb. Haemost., 13 Suppl 1, S115-S120 .
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| alpha2-antiplasmin + H2O | Yersinia pestis | alpha2AP is the main inhibitor of free plasmin in the circulation. Pla cleaves and inactivates alpha2AP by a single, rapid cut. It appears likely that the R376-M377 bait peptide bond is targeted by Pla | ? | - |
? |  |
| plasminogen + H2O | Yersinia pestis | activation | plasmin + ? | - |
? | |
| plasminogen activator inhibitor-1 + H2O | Yersinia pestis | inactivation. PAI-1 is the primary physiological inhibitor of uPA and t-PA and a major inhibitor of fibrinolysis. Pla rapidly inactivates PAI-1 by a single cleavage of the bait peptide at R346-M347. In circulation, most PAI-1 is bound to vitronectin, which is also degraded by Pla | ? | - |
? | |
| single-chain urokinase + H2O | Yersinia pestis | activation | ? | - |
? | |
| TAFI + H2O | Yersinia pestis | TAFI is secreted into plasma as a procarboxypeptidase, it is a regulatory protein linking the coagulation and fibrinolytic systems, and TAFI is protective in septic yersionosis. Pla cleaves at the C-terminal region of TAFI and reduces its activation to TAFIa | TAFIa + ? | - |
? | |
| tissue factor pathway inhibitor + H2O | Yersinia pestis | TFPI is a major anticoagulant and forms stable TFPI-FXa complexes that block blood clotting. Enzyme Pla cleaves the tissue factor pathway inhibitor, TFPI | ? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Yersinia pestis | P17811 | - |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| alpha2-antiplasmin + H2O | inactivation | Yersinia pestis | ? | - |
? | |
| alpha2-antiplasmin + H2O | alpha2AP is the main inhibitor of free plasmin in the circulation. Pla cleaves and inactivates alpha2AP by a single, rapid cut. It appears likely that the R376-M377 bait peptide bond is targeted by Pla | Yersinia pestis | ? | - |
? | |
| plasminogen + H2O | activation | Yersinia pestis | plasmin + ? | - |
? | |
| plasminogen activator inhibitor-1 + H2O | inactivation | Yersinia pestis | ? | - |
? | |
| plasminogen activator inhibitor-1 + H2O | inactivation. PAI-1 is the primary physiological inhibitor of uPA and t-PA and a major inhibitor of fibrinolysis. Pla rapidly inactivates PAI-1 by a single cleavage of the bait peptide at R346-M347. In circulation, most PAI-1 is bound to vitronectin, which is also degraded by Pla | Yersinia pestis | ? | - |
? | |
| single-chain urokinase + H2O | activation | Yersinia pestis | ? | - |
? | |
| TAFI + H2O | inactivation | Yersinia pestis | TAFIa + ? | - |
? | |
| TAFI + H2O | TAFI is secreted into plasma as a procarboxypeptidase, it is a regulatory protein linking the coagulation and fibrinolytic systems, and TAFI is protective in septic yersionosis. Pla cleaves at the C-terminal region of TAFI and reduces its activation to TAFIa | Yersinia pestis | TAFIa + ? | - |
? | |
| tissue factor pathway inhibitor + H2O | inactivation | Yersinia pestis | ? | - |
? | |
| tissue factor pathway inhibitor + H2O | TFPI is a major anticoagulant and forms stable TFPI-FXa complexes that block blood clotting. Enzyme Pla cleaves the tissue factor pathway inhibitor, TFPI | Yersinia pestis | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| Pla | - |
Yersinia pestis |
Expression
| Organism | Comment | Expression |
|---|---|---|
| Yersinia pestis | expression of Pla is partially repressed in glucose-containing medium | down |
| Yersinia pestis | transcription of pla is controlled by the cAMP receptor protein Crp | additional information |
General Information
| General Information | Comment | Organism |
|---|---|---|
| metabolism | plasminogen is an abundant circulating zymogen of the serine protease plasmin, which is the key enzyme in fibrinolysis. The physiological plasminogen activation by uPA (EC 3.4.21.73) or tPA (EC 3.4.21.68) is a single cut at the peptide bond R560-V561, which yields the two-chain active plasmin enzyme. Pla rapidly cleaves the same peptide as do the human physiological activators, and the formed plasmin remains enzymatically active as Pla does not degrade the B chain of plasmin that contains the protease catalytic domain | Yersinia pestis |
| physiological function | Pla of the enteropathogen Yersinia pestis is a surface-exposed, transmembrane beta-barrel proteases of the omptin family that exhibit a complex array of interactions with the hemostatic systems in vitro, the protease is an established virulence factor. Pla favors fibrinolysis by direct activation of plasminogen, inactivation of the serpins plasminogen activator inhibitor-1 and alpha2-antiplasmin, inactivation of the thrombin-activable fibrinolysis inhibitor, and activation of single-chain urokinase. Inactivation of alpha2AP enables proteolysis by the Pla-generated plasmin. The enzymatic activity of the protease is strongly influenced by the environment-induced variations in lipopolysaccharide that binds to the beta-barrel. The protease cleaves the tissue factor pathway inhibitor and thus also expresses procoagulant activity. Some of the functions observed for Pla, such as adhesiveness to laminin and invasiveness into human cells as well as efficient plasmin generation are not shown by PgtE (EC 3.4.23.49) or OmpT. Pla is adapted to support efficient plasminogen activation in the bubonic plague and to enhance bacterial survival in the lungs | Yersinia pestis |
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