3.4.23.48: plasminogen activator Pla
This is an abbreviated version!
For detailed information about plasminogen activator Pla, go to the full flat file.
Word Map on EC 3.4.23.48
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3.4.23.48
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aureus
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staphylococci
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methicillin-resistant
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microbiological
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methicillin
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vancomycin
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nosocomial
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epidermidis
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gentamicin
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mastitis
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catheter
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enterotoxin
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oxacillin
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swab
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ciprofloxacin
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bacteriological
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cocci
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amikacin
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clindamycin
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enterococci
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saprophyticus
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haemolyticus
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staph
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bacteremia
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methicillin-susceptible
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catheter-related
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viridans
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mupirocin
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tsst-1
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antibiograms
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linezolid
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xylosus
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kirby-bauer
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panton-valentine
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hyicus
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ceftazidime
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thermonuclease
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cefoxitin
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analysis
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medicine
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leukocidin
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teicoplanin
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methicillin-sensitive
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endophthalmitis
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warneri
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fusidic
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sccmec
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toxin-1
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imipenem
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ca-mrsa
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bactec
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capitis
- 3.4.23.48
- aureus
-
staphylococci
-
methicillin-resistant
-
microbiological
- methicillin
- vancomycin
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nosocomial
- epidermidis
- gentamicin
- mastitis
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catheter
- enterotoxin
- oxacillin
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swab
- ciprofloxacin
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bacteriological
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cocci
- amikacin
- clindamycin
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enterococci
- saprophyticus
- haemolyticus
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staph
- bacteremia
-
methicillin-susceptible
-
catheter-related
- viridans
- mupirocin
-
tsst-1
-
antibiograms
- linezolid
- xylosus
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kirby-bauer
-
panton-valentine
- hyicus
- ceftazidime
- thermonuclease
- cefoxitin
- analysis
- medicine
-
leukocidin
- teicoplanin
-
methicillin-sensitive
- endophthalmitis
- warneri
-
fusidic
-
sccmec
-
toxin-1
- imipenem
-
ca-mrsa
-
bactec
- capitis
Reaction
Converts human Glu-plasminogen to plasmin by cleaving the Arg560-/-Val peptide bond that is also hydrolysed by the mammalian u-plasminogen activator and t-plasminogen activator. Also cleaves arginyl bonds in other proteins =
Synonyms
beta-Pla, coagulase, fibrinolysin, outer membrane protease, Pla, Pla protease, plasminogen activator, plasminogen activator Pla, plasminogen activator protease Pla, YapE
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3.4.23.48 plasminogen activator PlaAdvanced search results
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Natural Substrates Products on EC 3.4.23.48 - plasminogen activator Pla
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NATURAL SUBSTRATE 
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
C3 protein of complement system + H2O
fragments of C3 protein of complement system
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?
TAFI + H2O
TAFIa + ?
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
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?
tissue factor pathway inhibitor + H2O
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TFPI is a major anticoagulant and forms stable TFPI-FXa complexes that block blood clotting. Enzyme Pla cleaves the tissue factor pathway inhibitor, TFPI
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?
YapE + H2O
?
Yersinia pestis autotransporter YapE protein
cleavage of YapE occurs in Yersinia pestis but not in the enteric Yersinia species, and requires the omptin Pla
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?
YapG + H2O
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Yersinia pestis autotransporter YapG protein
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
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?
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
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?
plasminogen + H2O
plasmin + ?
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capacity to convert plasminogen into plasmin by the action of the outer-membrane Lpa protein determined
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?
plasminogen + H2O
plasmin + ?
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capacity to convert plasminogen into plasmin by the action of the outer-membrane Lpa protein determined
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?
plasminogen + H2O
plasmin + ?
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activates plasminogen by cleaving the Arg560-Val561 bond
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?
plasminogen + H2O
plasmin + ?
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Pla also expresses a weak coagulase activity
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?
plasminogen + H2O
plasmin + ?
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activates plasminogen by cleaving the Arg560-Val561 bond
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?
plasminogen + H2O
plasmin + ?
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Pla has the additional ability to bind to the basement membrane component type IV collagen rendering adhesive properties to Yersina pestis cells
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?
plasminogen + H2O
plasmin + ?
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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
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plasminogen + H2O
plasmin + ?
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plasminogen activator is a surface virulence factor that contributes to the highly imvasive nature of the pathogen by binding various tissue matrix components
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plasminogen activator inhibitor-1 + H2O
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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
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?
plasminogen activator inhibitor-1 + H2O
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PAI-1 is cleaved and inactivated by the Pla protease of Yersinia pestis in the lung airspace of C57BL/6 mice
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?
plasminogen activator inhibitor-1 + H2O
?
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PAI-1 is cleaved and inactivated by the Pla protease of Yersinia pestis in the lung airspace of C57BL/6 mice
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?
additional information
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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
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?
additional information
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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
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additional information
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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
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