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Enzyme Nomenclature
Information on EC 3.4.23.48 - plasminogen activator Pla
for references in articles please use BRENDA:EC3.4.23.48
Word Map on EC 3.4.23.48
- 3.4.23.48
- yersinia
- pestis
- plague
-
pneumonic
-
bubonic
-
fibrinolytic
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dissemination
- omptins
- pulmonary
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beta-barrel
-
hemostatic
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alpha2-antiplasmin
- analysis
- enterica
-
adhesin
-
outgrowth
-
intranasal
-
pandemics
-
matrigel
-
pesticin
-
enterobacterial
-
enteropathogenic
- microtus
- pseudotuberculosis
-
laminin
-
basement
-
adhesiveness
- medicine
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
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EC NUMBER 
COMMENTARY 
3.4.23.48
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RECOMMENDED NAME
GeneOntology No.
plasminogen activator Pla
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
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
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-
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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
distribution of residues within the active site cleft strongly suggests that the arginine side chain of the substrate will bind in a deep, negatively charged pocket formed by Pla residues E29, D204, D206, and E217. The two valine residues C-terminal to the scissile bond will likely bind in the shallow, hydrophobic pocket located on the other side of the plane formed by the active site residues D84, H208, and the nucleophilic water molecule
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
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-
-
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CAS REGISTRY NUMBER
COMMENTARY
101028-08-4
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
intracellularly grown in Acanthamoeba castellanii ATCC 30234
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-
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638920, 638924, 638925, 668672, 668759, 668991, 669113, 670148, 695656, 698832, 734331, 734631, 735081
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expression of Pla enhances bacterial adhesiveness to basement membranes and to laminin; Pla is encoded on the 9.5 kb pesticin or Pst plasmid pPCP1
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non-pigmented avirulent strain of Yersinia pestis KIM, substrain D28, expressing plasminogen activator Pla and its pPCP-cured version, substrain D47
SwissProt
Pla mediates bacterial invasion into human endothelial cells independently of its proteolytic activity
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wild-type strain CO92, isogenic strain lacking Pla (CO92 DELTA-pla) and complemented CO92 DELTA-pla strain
SwissProt
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
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Yersinia pestis binding to fibronectin is mediated through Ail protein and plasminogen activator Pla
physiological function
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the outer membrane plasminogen activator Pla of Yersinia pestis is a central virulence factor in plague
physiological function
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the plasminogen activator Pla single and the Braun lipoprotein Lpp Pla double mutant are unable to survive efficiently in murine and human macrophages. The levels of Pla and its associated protease activity are not affected in the Lpp single mutant, and, likewise, deletion of the Pla gene from wild-type does not alter Lpp levels. The ability of the Lpp Pla double mutant to be phagocytized by macrophages, to stimulate production of tumor necrosis factor-alpha and interleukin-6, and to activate the nitric oxide killing pathways of the host cells remains unaltered when compared to the wild-type-infected macrophages. Macrophages infected with either the wild-type or the Lpp Pla double mutant are equally efficient in their uptake of zymosan particles
physiological function
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cleavage of Yersinia pestis autotransporter YapE by protease Pla is required to mediate bacterial aggregation and adherence to eukaryotic cells. Post-translation modification of YapE appears to be specific to Yersinia pestis. It was acquired along with the acquisition ofplasmid pPCP1 during the divergence of Yersinia pestis from Yersinia pseudotuberculosis, and is the first evidence of a mechanism to regulate bacterial adherence
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SUBSTRATE
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
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
-
?
C3 protein of complement system + H2O
fragments of C3 protein of complement system
-
-
-
-
-
C3 protein of complement system + H2O
fragments of C3 protein of complement system
-
-
-
?
D-Val-Leu-Lys-p-nitroanilide + H2O
D-Val-Leu-Lys + p-nitroaniline
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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
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-
?
D-Val-Leu-Lys-p-nitroanilide + H2O
D-Val-Leu-Lys + p-nitroaniline
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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
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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 + ?
-
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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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 + ?
-
activates plasminogen by cleaving the Arg560-Val561 bond
-
?
plasminogen + H2O
plasmin + ?
-
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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-
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plasminogen + H2O
plasmin + ?
-
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 + H2O
plasmin + ?
identification and analysis of small-peptide substrates and inhibitors of plasminogen activator Pla by use of parallel synthesis and positional scanning
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-
?
plasminogen + H2O
plasmin + ?
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
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-
?
Yersinia outer proteins + H2O
fragments of Yersinia outer proteins
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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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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
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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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NATURAL SUBSTRATES
NATURAL PRODUCTS
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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-
-
-
-
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
-
?
YapG + H2O
?
-
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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?
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 + ?
-
capacity to convert plasminogen into plasmin by the action of the outer-membrane Lpa protein determined
-
-
?
plasminogen + H2O
plasmin + ?
-
activates plasminogen by cleaving the Arg560-Val561 bond
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-
-
plasminogen + H2O
plasmin + ?
-
Pla also expresses a weak coagulase activity
-
-
-
plasminogen + H2O
plasmin + ?
-
activates plasminogen by cleaving the Arg560-Val561 bond
-
-
-
plasminogen + H2O
plasmin + ?
-
Pla has the additional ability to bind to the basement membrane component type IV collagen rendering adhesive properties to Yersina pestis cells
-
-
-
plasminogen + H2O
plasmin + ?
-
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
-
-
-
plasminogen + H2O
plasmin + ?
-
plasminogen activator is a surface virulence factor that contributes to the highly imvasive nature of the pathogen by binding various tissue matrix components
-
-
?
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
-
-
-
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
-
-
-
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
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-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
-
plasminogen activator is upregulated at 37°C with calcium (2.4fold) and at 37°C without Ca2+ (2.8fold) compared to the case at 26°C with calcium
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
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WSLLTPAand YPYIPLT inhibit laminin binding activity of plasmonogen activator
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additional information
potential small-peptide inhibitors of plasminogen activator Pla screened by parallel synthesis and positional scanning, selected small-peptide substrates analyzed by examining ability to inhibit the conversion of plasminogen to plasmin in a fibrin plate assay and by application of a fluorimetric assay
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
expression of Lpa gene shown in exponential and stationary growth phase, transcription shown to be directed by own promoter
additional information
peptide synthesis described, DABCYL/EDANS quencher/fluorophor system used, minimal substrate length determined, positional scan approach applied, peptide sequences tested as substrates and functional inhibitors listed, kinetics of cleavage of identified fluorescent substrates shown, fluorimetric assay and fibrinolytic assay applied, analysis of six-residue peptides and optimization studies of potential tripeptide substrates performed, inhibitory activity od selectetes small-peptides analyzed
additional information
kinetics of infection summarized, lack of plasminogen activator Pla shown to delay the time to death resulting from respiratory infection of mice, plasminogen activator Pla shown to control proliferation of Yersinia pestis in the lungs but is not essential for bacteria to disseminate, aborted inflammation and activated lung repair shown in absence of expression of plasminogen activator Pla
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
26 - 37
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plasminogen activator is upregulated at 37°C with calcium (2.4fold) and at 37°C without Ca2+ (2.8fold) compared to the case at 26°C with calcium
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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PDB
SCOP
CATH
ORGANISM
UNIPROT
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
31000
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plasminogen activator Pla exhibits three molecular forms: alpha-Pla with an MW of 35000 Da, beta-Pla of 33000 Da and gamma-Pla with 31000 Da. the formation of beta-Pla from alpha-Pla results from autoprocessing at the residue Lys262. gamma-Pla most likely represents full-size mature Pla that has folded differently from alpha-Pla
32600
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alpha-Pla, x * 32600, a transient 34600 Da primary Pla product is processed upon insertion into the outer membrane to yield alpha-Pla, deduced from nucleotide sequence
33000
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plasminogen activator Pla exhibits three molecular forms: alpha-Pla with an MW of 35000 Da, beta-Pla of 33000 Da and gamma-Pla with 31000 Da. the formation of beta-Pla from alpha-Pla results from autoprocessing at the residue Lys262. gamma-Pla most likely represents full-size mature Pla that has folded differently from alpha-Pla
35000
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plasminogen activator Pla exhibits three molecular forms: alpha-Pla with an MW of 35000 Da, beta-Pla of 33000 Da and gamma-Pla with 31000 Da. the formation of beta-Pla from alpha-Pla results from autoprocessing at the residue Lys262. gamma-Pla most likely represents full-size mature Pla that has folded differently from alpha-Pla
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
alpha-Pla, x * 32600, a transient 34600 Da primary Pla product is processed upon insertion into the outer membrane to yield alpha-Pla, deduced from nucleotide sequence
additional information
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Pla occurs in 3 processed forms of alpha-Pla, beta-Pla and gamma-Pla, of which alpha-Pla with an apparant molecular mass of 37000 Da, corresponds to full-size mature Pla, and beta-Pla and gamma-Pla with molecular weights of 31000 Da and 35000 Da respectively, are thought to result from processing of alpha-Pla, beta-Pla may result from an autoprocessing event
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
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plasminogen activator Pla is autoprocessed at the C-terminus. This does not enhance plasminogen activation
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
co-crystal structure of lipopolysaccharide-free Pla in complex with the activation loop peptide of human plasminogen, its natural substrate. The structure shows that in the absence of lipopolysaccharide, the peptide substrate binds deep within the active site groove and displaces the nucleophilic water molecule, leading to inactivation
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comparison of the structure of Pla and the modeled structure of protease Epo of the plant pathogenic Erwinia pyrifoliae
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molecular dynamics simulation of interaction with plasminogen. After a total of 8 ns, the predicted docked complex of plasminogen-palsminogen activator Pla shows the relaxation of the beta-barrel structure of Pla and the progressive approximation and stabilization between the cleavage site of plasmnogen into the extracellular loops of Pla, followed by the increase in the number of H bonds
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wild-type, to 1.9 A, and inactive mutant D86A, to 2.5 A resolution, respectively. The structure shows a water molecule located between active site residues D84 and H208, and a number of other water molecules. The R211 side-chain in loop L4 is close to the nucleophilic water and possibly involved in the stabilization of the oxyanion intermediate. Subtle conformational changes of H208 result from the binding of lipopolysaccharide to the outside of the barrel, explaining the unusual dependence of omptins on lipopolysaccharide for activity
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purification of a His6-tagged fusion protein from Escherichia coli and reconstitution with lipopolysaccharide to an enzymatically active form. Purified His-tagged enzyme is coated onto fluorescent micro-particles and expresses plasminogen activity. The enzyme molecules have intrinsic adhesive properties. The purified transmembrane proteins coated onto fluorescence micro-particles can be used for functional assays
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
BL21-DE3 used as a host to express recombinant protein, cloning into pBluescript SK+ to produce plasmid pBLA4L
expressed in Escherichia coli TG1, strains BL21 and BL21(DE3)pLys used for expression of recombinant proteins
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tetracycline-responsive promoter system in Yersinia pestis applied to control primary pneumonic plague progression after activation/inhibition of plasminogen activator Pla expression
the mutant enzyme T259I is expressed in Escherichia coli XL1 Blue cells and in Yersinia pestis strain KIM D34
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D206A
D86A
S99A
T259I
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the substitution impairs fibrinolytic activity and plasminogen activation
additional information
additional information
-
the acyltransferase gene mutant lpxM has an altered activity of plasminogen activator Pla
additional information
-
swapping of ten amino acid residues at two surface loops of Pla and membrane protease Epo of the plant pathogenic Erwinia pyrifoliae introduces plasminogen activation capacity in Epo and inactivates the function in Pla
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
medicine
-
the Lpp Pla double mutant of Yersinia pestis CO92 is highly attenuated and it retains the ability to elicit innate and subsequent acquired immune responses in the host similar to that of wild-type CO92, which are highly desirable in a live-attenuated vaccine candidate
analysis
-
multiplex real-time polymerase chain reaction assay for the detection of Yersinia pestis and Yersinia pseudotuberculosis using the Yersinia pestis pla gene coding for plasminogen activator and the ypo2088 gene. Assays are both sensitive and specific, the lower detection limit is 10-100 fg of extracted total DNA
analysis
-
development of a highly sensitive one-step PLA-enzyme immunoassay and an immunostrip, usable as a rapid test under field conditions. The PLA-immunometric tests allow a rapid and easy detection of Yersinia pestis in environmental and flea samples
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