3.4.23.48 (DABCYL)-Arg-Arg-Ile-Asn-Arg-Glu-(EDANS)-NH2 + H2O - Yersinia pestis subsp. microtus (DABCYL)-Arg + Arg-Ile-Asn-Arg-Glu-(EDANS)-NH2 - ? 449107 3.4.23.48 (DABCYL)-Arg-Arg-Ile-Asn-Arg-Glu-(EDANS)-NH2 + H2O - Yersinia pestis subsp. pestis (DABCYL)-Arg + Arg-Ile-Asn-Arg-Glu-(EDANS)-NH2 - ? 449107 3.4.23.48 (DABCYL)-Arg-Arg-Ile-Asn-Arg-Glu-(EDANS)-NH2 + H2O - Yersinia pestis subsp. microtus 91001 (DABCYL)-Arg + Arg-Ile-Asn-Arg-Glu-(EDANS)-NH2 - ? 449107 3.4.23.48 alpha2-antiplasmin + H2O inactivation Yersinia pestis ? - ? 391266 3.4.23.48 alpha2-antiplasmin + H2O Pla inactivates the main physiologic inhibitor of plasmin Yersinia pestis ? - ? 391266 3.4.23.48 alpha2-antiplasmin + H2O Pla inactivates alpha2-antiplasmin Yersinia pestis ? - ? 391266 3.4.23.48 alpha2-antiplasmin + H2O a serpin Yersinia pestis ? - ? 391266 3.4.23.48 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 ? - ? 391266 3.4.23.48 C3 protein of complement system + H2O - Yersinia pestis fragments of C3 protein of complement system - ? 355652 3.4.23.48 complement C3 + H2O Pla proteolyzes complement C3 which may amiliorate the host inflammatory response by abolishing its chemoattractant properties Yersinia pestis ? - ? 411888 3.4.23.48 complement protein C3 + H2O - Yersinia pestis ? - ? 384465 3.4.23.48 D-Val-Leu-Lys-p-nitroanilide + H2O Lpa gene encoding a homologue of the plasminogen activator Pla of Yersinia pestis identified, described as a surface protease exhibiting plasminogen activator activity, plasminogen activity of inner and outer membranes measured Legionella pneumophila D-Val-Leu-Lys + p-nitroaniline - ? 36961 3.4.23.48 D-Val-Leu-Lys-p-nitroanilide + H2O Lpa gene encoding a homologue of the plasminogen activator Pla of Yersinia pestis identified, described as a surface protease exhibiting plasminogen activator activity, plasminogen activity of inner and outer membranes measured Legionella pneumophila Philadelphia D-Val-Leu-Lys + p-nitroaniline - ? 36961 3.4.23.48 human alpha2-antiplasmin + H2O - Yersinia pestis fragments of alpha2-antiplasmin - ? 370486 3.4.23.48 human Glu-plasminogen + H2O Pla activates Glu-plasminogen to plasmin, in vitro, TFPI is found to be a much better substrate for Pla than plasminogen Yersinia pestis plasmin + ? - ? 412175 3.4.23.48 human tissue factor pathway inhibitor + H2O Pla can proteolytically degrade TFPI, completely abrogating its anticoagulant function. In vitro, TFPI is found to be a much better substrate for Pla than plasminogen Yersinia pestis ? - ? 412177 3.4.23.48 additional information plasminogen activator Pla is essential for the spread of Yersinia pestis from the subcutaneous infection site into circulation, and the proteolytic activation of plasminogen is involved in virulence function. In addition to proteolysis plasminogen activator Pla promotes bacterial adhesion to mammalian extracellular matrices and epithelial cells as well as bacterial invasion into eukayotic cells. Laminin functions as an adhesion target for plasminogen activator Pla, which also expresses a lower adhesion affinity for heparan sulfate proteoglycan. the adhesion targets are not directly degraded by plasminogen activator Pla, but Pla-mediated generation of plasmin leads to their degradation Yersinia pestis ? - ? 89 3.4.23.48 additional information plasminogen activator plays a pivotal role in internalisation of bacteria by HeLa cells. Intracellular signalling and cytoskeletal rearrangement is involved in Yersinia pestis plasminogen activator mediated HeLa cell invasion Yersinia pestis ? - ? 89 3.4.23.48 additional information no degradation of Val-Leu-Lys-p-nitroanilide. Plasminogen activator degrades outer membrane proteins of Yersinia cell surface and exhibits a weak coagulase activity. In addition to proteolysis plasminogen activator Pla promotes bacterial adhesion to mammalian extracellular matrices and epithelial cells as well as bacterial invasion into eukaryotic cells. Laminin functions as an adhesion target for plasminogen activator Pla, which also expresses a lower adhesion affinity for heparan sulfate proteoglycan. The adhesion targets are not directly degraded by plasminogen activator Pla, but Pla-mediated generation of plasmin leads to their degradation Yersinia pestis ? - ? 89 3.4.23.48 additional information the enzyme performs autoproteolysis Yersinia pestis subsp. microtus ? - ? 89 3.4.23.48 additional information the enzyme performs autoproteolysis Yersinia pestis subsp. pestis ? - ? 89 3.4.23.48 additional information the invasion of alveolar macrophages by Yersinia pestis depends both in vitro and in vivo on the expression of plasminogen activator Pla. Macrophages and transfectants expressing C-type lectin receptor DEC-205, but not their negative counterparts, phagocytose plasminogen activator Pla-expressing Yersinia pestis and Escherichia coli K12 more efficiently than Pla-negative controls. The interactions between Pla-expressing bacteria and DEC-205-expressing transfectants or alveolar macrophages can be inhibited by an anti-DEC-205 antibody. The blockage of the Pla-DEC-205 interaction reduces the dissemination of Yersinia pestis in mice Yersinia pestis ? - ? 89 3.4.23.48 additional information the enzyme performs autoproteolysis Yersinia pestis subsp. microtus 91001 ? - ? 89 3.4.23.48 PAI-1 + H2O a serpin Yersinia pestis ? - ? 418989 3.4.23.48 plasminogen + H2O - Yersinia pestis plasmin + ? - ? 15549 3.4.23.48 plasminogen + H2O Pla also expresses a weak coagulase activity Yersinia pestis plasmin + ? - ? 15549 3.4.23.48 plasminogen + H2O activates plasminogen by cleaving the Arg560-Val561 bond Mammalia plasmin + ? - ? 15549 3.4.23.48 plasminogen + H2O activates plasminogen by cleaving the Arg560-Val561 bond Yersinia pestis plasmin + ? - ? 15549 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 Yersinia pestis plasmin + ? - ? 15549 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 Yersinia pestis plasmin + ? - ? 15549 3.4.23.48 plasminogen + H2O activation Yersinia pestis plasmin + ? - ? 15549 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 Yersinia pestis plasmin + ? - ? 15549 3.4.23.48 plasminogen + H2O cleavage of Arg560-/-Val561 Yersinia pestis plasmin + ? - ? 15549 3.4.23.48 plasminogen + H2O capacity to convert plasminogen into plasmin by the action of the outer-membrane Lpa protein determined Legionella pneumophila plasmin + ? - ? 15549 3.4.23.48 plasminogen + H2O identification and analysis of small-peptide substrates and inhibitors of plasminogen activator Pla by use of parallel synthesis and positional scanning Yersinia pestis plasmin + ? - ? 15549 3.4.23.48 plasminogen + H2O plasminogen activator Pla shown to be essential to cause primary pneumonic plague, minor importance determined for dissemination during pneumonic plague than during bubonic plague, inhibition of plasminogen activator Pla expression shown to prolong survival of infected mice Yersinia pestis plasmin + ? - ? 15549 3.4.23.48 plasminogen + H2O capacity to convert plasminogen into plasmin by the action of the outer-membrane Lpa protein determined Legionella pneumophila Philadelphia plasmin + ? - ? 15549 3.4.23.48 plasminogen activator inhibitor-1 + H2O - Yersinia pestis ? - ? 394476 3.4.23.48 plasminogen activator inhibitor-1 + H2O inactivation Yersinia pestis ? - ? 394476 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 Yersinia pestis ? - ? 394476 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 Yersinia pestis ? - ? 394476 3.4.23.48 plasminogen activator inhibitor-1 + H2O - Yersinia pestis CO92 ? - ? 394476 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 Yersinia pestis CO92 ? - ? 394476 3.4.23.48 serpin alpha2-antiplasmin + H2O - Yersinia pestis ? - ? 385727 3.4.23.48 single-chain urokinase + H2O activation Yersinia pestis ? - ? 448940 3.4.23.48 TAFI + H2O inactivation Yersinia pestis TAFIa + ? - ? 448981 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 Yersinia pestis TAFIa + ? - ? 448981 3.4.23.48 tissue factor pathway inhibitor + H2O inactivation Yersinia pestis ? - ? 367349 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 Yersinia pestis ? - ? 367349 3.4.23.48 YapE + H2O Yersinia pestis autotransporter YapE protein Yersinia pestis ? cleavage of YapE occurs in Yersinia pestis but not in the enteric Yersinia species, and requires the omptin Pla ? 432980 3.4.23.48 YapG + H2O Yersinia pestis autotransporter YapG protein Yersinia pestis ? sites K512, (K548-R549) and K594-R595 represent the primary cleavage sites of YapG, whereas sites K'558 and K'604 represent the secondary alternative cleavage sites ? 432981 3.4.23.48 Yersinia outer proteins + H2O - Yersinia pestis fragments of Yersinia outer proteins - ? 355653 3.4.23.48 zymogen factor VII + H2O Pla proteolytically converts zymogen factor VII to the active form, factor VIIa. Pla activates factor VII about twice as fast as it activates plasminogen Yersinia pestis factor VIIa - ? 366569