EC Number   |
Natural Substrates |
|---|
   3.4.23.48 | plasminogen + H2O |
Pla has the additional ability to bind to the basement membrane component type IV collagen rendering adhesive properties to Yersina pestis cells |
| 3.4.23.48 | plasminogen + H2O |
Pla belongs to the omptin family of enterobacterial surface proteases and is responsible for the highly efficient invasion of the plague bacterium from the subcutaneous infection site into the circulation |
| 3.4.23.48 | plasminogen + H2O |
activation |
| 3.4.23.48 | plasminogen + H2O |
plasminogen activator is a surface virulence factor that contributes to the highly imvasive nature of the pathogen by binding various tissue matrix components |
| 3.4.23.48 | plasminogen + H2O |
capacity to convert plasminogen into plasmin by the action of the outer-membrane Lpa protein determined |
| 3.4.23.48 | 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 |
| 3.4.23.48 | plasminogen activator inhibitor-1 + H2O |
PAI-1 is cleaved and inactivated by the Pla protease of Yersinia pestis in the lung airspace of C57BL/6 mice |
| 3.4.23.48 | single-chain urokinase + H2O |
activation |
| 3.4.23.48 | 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 |
| 3.4.23.48 | 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 |
