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Information on EC 3.4.24.26 - pseudolysin and Organism(s) Pseudomonas aeruginosa and UniProt Accession P14756
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3.4.24.26 pseudolysinSpecify your search results
Word Map
- 3.4.24.26
- thermolysin
- metalloproteinases
- collagenase
- metalloprotease
-
3.4.24.4
- elastin
- gelatinase
- elastases
- phosphoramidon
-
pseudomonal
- stromelysin
-
thermolysin-like
- metalloendopeptidase
- medicine
- thermoproteolyticus
- aureolysin
- vibriolysin
-
intrastromal
- industry
- nutrition
- biotechnology
- synthesis
- pharmacology
- diagnostics
The taxonomic range for the selected organisms is: Pseudomonas aeruginosa
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Hydrolysis of proteins including elastin, collagen types III and IV, fibronectin and immunoglobulin A, generally with bulky hydrophobic group at P1'. Insulin B chain cleavage pattern identical to that of thermolysin, but specificity differs in other respects
Synonyms
pseudomonas aeruginosa elastase, pseudolysin, neutral metalloproteinase, pseudomonas elastase, elastase b, pseudomonas protease, aeruginolysin, elastolytic metalloproteinase, lasb protease, a2 elastase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Pseudomonas aeruginosa elastase
-
elastase
LasB protease
Neutral metalloproteinase
-
-
-
-
Pseudomonas aeruginosa elastase
-
-
Pseudomonas aeruginosa neutral metalloproteinase
-
-
-
-
Pseudomonas elastase
additional information
PAE is a metalloprotease of the M4 peptidase family
elastase
-
-
-
-
Pseudomonas elastase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
171715-23-4
-
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
2-aminobenzoyl-Ala-Gly-Leu-Ala-4-nitrobenzylamide + H2O
?
25°C, pH 7.4
-
-
?
3-(2-furyl)acryloyl-glycyl-L-phenylalanyl-L-phenylalanine + H2O
L-phenylalanyl-L-phenylalanine + 3-(2-furyl)acryloyl-glycine
at 37°C, pH 7.3
-
-
?
alpha1-proteinase inhibitor + H2O
?
25°C, pH 7.4, cleavage occurs at the Pro357-Met358 bond (wild-type and recombinant Met358 inhibitor) and at the Pro357-Leu358 bond (recombinant mutant M358L inhibitor)
-
-
?
carbobenzooxydialanine-leucylalaninamide + H2O
?
30°C, pH 8.6
-
-
?
carbobenzooxydialanine-phenylalanylalaninamide + H2O
?
30°C, pH 8.6
-
-
?
carbobenzooxydialanine-tyrosylalaninamide + H2O
?
30°C, pH 8.6
-
-
?
cartilage + H2O
?
major components proteoglycans and collagen
-
-
?
furylacryloyl-Gly-Leu-NH2 + H2O
furylacryloyl-Gly + Leu-NH2
pH 7.5, 23-25°C
-
-
?
human gamma-interferon + H2O
fragments of human gamma-interferon
-
-
-
?
monocyte-derived alpha1-antitrypsin + H2O
?
37°C
51-kD polypeptide
-
?
N-chlorosuccinimide-oxidized inhibitor + H2O
?
25°C, pH 7.4, cleavage occurs between Glu354 and Ala355
-
-
?
proteinase-activated receptor 2 + H2O
?
the enzyme cleaves proteinase-activated receptor 2 to remove the extracellular Flag epitope
-
-
?
2-Aminobenzoyl-Ala-Gly-Leu-Ala 4-nitrobenzylamide + H2O
2-Aminobenzoyl-Ala-Gly + Leu-Ala 4-nitrobenzylamide
AAF-7-amido-4-methylcoumarin + H2O
AAF + 7-amino-4-methylcoumarin
-
-
-
-
?
Ac-DEVD-7-amido-4-methylcoumarin + H2O
Ac-DEVD + 7-amino-4-methylcoumarin
-
-
-
-
?
Boc-GKR-7-amido-4-methylcoumarin + H2O
Boc-GKR + 7-amino-4-methylcoumarin
-
-
-
-
?
Boc-QAR-7-amido-4-methylcoumarin + H2O
Boc-QAR + 7-amino-4-methylcoumarin
-
-
-
-
?
Boc-VLK-7-amido-4-methylcoumarin + H2O
Boc-VLK + 7-amino-4-methylcoumarin
-
-
-
-
?
Boc-VPR-7-amido-4-methylcoumarin + H2O
Boc-VPR + 7-amino-4-methylcoumarin
-
-
-
-
?
eggshell membrane + H2O
Val-Leu-Pro-Pro + (X)-Val-Pro-Pro + Trp + ?
-
-
-
-
?
elastase propeptide + H2O
elastase + ?
-
autocatalytically cleaved
-
?
flagellin + H2O
?
the enzyme is capable of degrading exogenous flagellin under calcium-replete conditions and prevents flagellin-mediated immune recognition
-
-
?
furylacryloyl-Gly-Leu-NH2 + H2O
furylacryloyl-Gly + Leu-NH2
-
poor substrate
-
?
interleukin-8 + H2O
?
-
rapid processing to a 72 amino acid form, further degradation is slow
-
-
?
methyl-O-Suc-AAPV-7-amido-4-methylcoumarin + H2O
methyl-O-Suc-AAPV + 7-amino-4-methylcoumarin
-
-
-
-
?
myeloma IgA2-lamda of A2m(2) allotype + H2O
?
-
predominantly polymeric, 37°C
-
-
?
N-succinyl-Ala-Ala-Ala-4-nitroanilide + H2O
N-succinyl-Ala-Ala-Ala + 4-nitroaniline
-
-
-
-
?
PAR2 + H2O
?
-
i.e. proteinase-activated receptor 2, enzyme cleaves the N-terminal domain of PAR2 from the cell surface without triggering receptor endocytosis as trypsin does. Cleavage does not activate PAR2, but disarms the recptor for subsequent activation by trypsin
-
?
PFR-7-amido-4-methylcoumarin + H2O
PFR + 7-amino-4-methylcoumarin
-
-
-
-
?
Suc-AAF-7-amido-4-methylcoumarin + H2O
Suc-AAF + 7-amino-4-methylcoumarin
-
-
-
-
?
Suc-AFK-7-amido-4-methylcoumarin + H2O
Suc-AFK + 7-amino-4-methylcoumarin
-
-
-
-
?
Suc-GPLGP-7-amido-4-methylcoumarin + H2O
Suc-GPLGP + 7-amino-4-methylcoumarin
-
-
-
-
?
Suc-IIW-7-amido-4-methylcoumarin + H2O
Suc-IIW + 7-amino-4-methylcoumarin
-
-
-
-
?
Suc-LLVY-7-amido-4-methylcoumarin + H2O
Suc-LLVY + 7-amino-4-methylcoumarin
-
-
-
-
?
Z-AAN-7-amido-4-methylcoumarin + H2O
Z-AAN + 7-amino-4-methylcoumarin
-
-
-
-
?
Z-GAH-7-amido-4-methylcoumarin + H2O
Z-GAH + 7-amino-4-methylcoumarin
-
-
-
-
?
Z-GAM-7-amido-4-methylcoumarin + H2O
Z-GAM + 7-amino-4-methylcoumarin
-
-
-
-
?
Z-GGL-7-amido-4-methylcoumarin + H2O
Z-GGL + 7-amino-4-methylcoumarin
-
-
-
-
?
Z-GGR-7-amido-4-methylcoumarin + H2O
Z-GGR + 7-amino-4-methylcoumarin
-
-
-
-
?
Z-LLE-7-amido-4-methylcoumarin + H2O
Z-LLE + 7-amino-4-methylcoumarin
-
-
-
-
?
Z-RLRGG-7-amido-4-methylcoumarin + H2O
Z-RLRGG + 7-amino-4-methylcoumarin
-
-
-
-
?
azocasein + H2O
?
proteolytic activity is 8 to 9fold lower than in the wild-type strain
-
-
?
Elastin + H2O
?
pseudolysin bound to bovine elastin fibers and preferred to attack peptide bonds with hydrophobic residues at the P1 and P1' positions in the hydrophobic domains of elastin
-
-
?
elastin Congo red + H2O
?
elastolytic activity is 14fold lower than in the wild-type strain
-
-
?
elastin Congo red + H2O
?
elastolytic activity is 20fold lower than in the wild-type strain
-
-
?
furylacryloyl-glycyl-L-leucyl-L-alanine + H2O
furylacryloyl-glycine + L-leucyl-L-alanine
25°C, pH 7.5
-
-
?
furylacryloyl-glycyl-L-leucyl-L-alanine + H2O
furylacryloyl-glycine + L-leucyl-L-alanine
pH 7.5, 25°C
-
-
?
human thrombin + H2O
?
digestion of thrombin by Pseudomonas aeruginosa elastase leads to the release of the C-terminal thrombin-derived peptide FYT21, which inhibits pro-inflammatory responses to several pathogen-associated molecular patterns in vitro and in vivo by preventing toll-like receptor dimerization and subsequent activation of down-stream signalling pathways the enzyme cleaves a C-terminal peptide from human thrombin that inhibits host inflammatory responses
-
-
?
2-Aminobenzoyl-Ala-Gly-Leu-Ala 4-nitrobenzylamide + H2O
2-Aminobenzoyl-Ala-Gly + Leu-Ala 4-nitrobenzylamide
-
-
-
-
?
2-Aminobenzoyl-Ala-Gly-Leu-Ala 4-nitrobenzylamide + H2O
2-Aminobenzoyl-Ala-Gly + Leu-Ala 4-nitrobenzylamide
-
-
-
?
additional information
?
-
key catalytic residues and residues at the S1 and S'1 binding subsites, reaction mechanism, overview
-
-
?
additional information
?
-
-
key catalytic residues and residues at the S1 and S'1 binding subsites, reaction mechanism, overview
-
-
?
additional information
?
-
-
with synthetic substrates of the general structure benzyloxycarbonyl-Phe-Xaa-Ala, the Phe-Xaa bond is cleaved, the decreasing order of preference for Xaa is as follows: Phe, Leu, Tyr, Val, Ile
-
-
?
additional information
?
-
-
specificity against aromatic or hydrophobic amino acid residues at the amino-side of the splitting point
-
-
?
additional information
?
-
-
probably responsible for the tissue destruction observed during pulmonary and corneal infections by the pathogen organism Pseudomonas aeruginosa
-
-
?
additional information
?
-
-
no activity with dabsyl-Leu-Gly-Gly-Gly-Ala-edans
-
-
?
additional information
?
-
-
enzyme prefers Ser at position P1, Lys at P2 and hydropobic amino acids at the P1' and P2' positions
-
-
?
additional information
?
-
-
large exopeptidase LepA activates nuclear factor kappa-kB-driven promoter through human protease activated receptors PAR-1, -2 or -4 and cleaves the peptides corresponding to the tethered ligand region of human PAR-1, -2 and -4 at a specific site with exposure of their tethered ligands
-
-
?
additional information
?
-
-
no substrate: N-succinyl-Ala-Ala-Ala-p-nitroanilide, N-succinyl-Ala-Pro-Ala-p-nitroanilide
-
-
?
additional information
?
-
-
non- and glycosylated isoforms of rPAE display similar kinetic parameters for hydrolyzing casein in aqueous medium, and when catalyzing bipeptide synthesis in 50% v/v DMSO, they exhibit identical substrate specificity and activity, and produce similar yields
-
-
?
additional information
?
-
-
the enzyme shows both hemolytic and hemorrhagic activities in vivo
-
-
?
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
human thrombin + H2O
?
digestion of thrombin by Pseudomonas aeruginosa elastase leads to the release of the C-terminal thrombin-derived peptide FYT21, which inhibits pro-inflammatory responses to several pathogen-associated molecular patterns in vitro and in vivo by preventing toll-like receptor dimerization and subsequent activation of down-stream signalling pathways the enzyme cleaves a C-terminal peptide from human thrombin that inhibits host inflammatory responses
-
-
?
flagellin + H2O
?
the enzyme is capable of degrading exogenous flagellin under calcium-replete conditions and prevents flagellin-mediated immune recognition
-
-
?
PAR2 + H2O
?
-
i.e. proteinase-activated receptor 2, enzyme cleaves the N-terminal domain of PAR2 from the cell surface without triggering receptor endocytosis as trypsin does. Cleavage does not activate PAR2, but disarms the recptor for subsequent activation by trypsin
-
?
additional information
?
-
-
probably responsible for the tissue destruction observed during pulmonary and corneal infections by the pathogen organism Pseudomonas aeruginosa
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Zinc
Zn2+
Ca2+
-
a calcium ion is also required for enzyme activity, and stabilizes its tertiary structure. Contact with the calcium ion is made by the carboxyl groups of Asp136, Glu172, Glu175, and Asp183, the carbonyl group of Leu185, and one water molecule
Zinc
Zn2+
additional information
Zn2+
PAE contains zinc, binding site structure, HEXXH is the putative signature of Zn-metalloproteases, overview
Zn2+
-
the enzyme is a metalloprotease that requires a zinc atom, bound to His140, His144, and Glu164, for its activity
Zn2+
zinc metalloproteinase. His140, His144 and Glu164 serve as ligands for zinc ion
additional information
-
Mg2+ and Ca2+ at 0.625 mM have no effect on the activity, Mn2+, Co2+, and Fe3+ at 0.625 mM partly inhibit the enzyme, Zn2+ and Cu2+ inhibit the enzyme completely
additional information
-
metalloprotease, the enzynme contains the typical metalloendopeptidases consensus zinc-binding sequence HEXXH
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-mercaptoacetyl-L-phenylalanyl-L-leucine
prevents corneal perforation completely
2-mercaptoacetyl-Phe-Leu
at 0.1 mM 96% inhibition with azocasein as substrate, 97% inhibition with elastin as substrate and 97% inhibition with cartilage as substrate, at 0.01 mM 77% inhibition with azocasein as substrate, 33% inhibition with elastin as substrate and 66% inhibition with cartilage as substrate
ammonium chloride
extracellular elastase activity decreases if cells are cultured in the presence of ammonium chloride
anti elastase monoclonal antibody
reduces PE activity significantly
-
benzyloxycarbonyl-Gly-NHOH
at 14 mM 98% inhibition with azocasein as substrate, 95% inhibition with elastin as substrate and 95% inhibition with cartilage as substrate, at 1.4 mM 77% inhibition with azocasein as substrate, 84% inhibition with elastin as substrate and 67% inhibition with cartilage as substrate
benzyloxycarbonyl-Leu-NHOH
at 5.0 mM 98% inhibition with azocasein as substrate, 100% inhibition with elastin as substrate and 94% inhibition with cartilage as substrate, at 0.5 mM 76% inhibition with azocasein as substrate, 93% inhibition with elastin as substrate and 57% inhibition with cartilage as substrate
D-glucose
extracellular elastase activity decreases if cells are cultured in the presence of glucose
N-(1-carboxy-3-phenylpropyl)-phenylalanyl-alpha-asparagine
enzyme binding structure analysis, PDB ID 1U4G. The inhibitor is bound in the S1-S1 sub-sites of pseudolysin by hydrogen bonding and hydrophobic and weak van der Waal's interactions
HS-CH2-CO-Phe-Tyr-NH2
-
at 0.2 mM and 0.025 mM inhibits the degradation of the pseudolysin natural substrates nucleoside diphosphate kinase and IgG, respectively
HSAc-Leu-Phe
-
0.1 mM, inhibits 97% of the degradation of azocasein and elastin substrates by pseudolysin
HSAc-Phe-Leu
-
0.1 mM, inhibits 97% of the degradation of azocasein and elastin substrates by pseudolysin
peptides
-
containing the hydroxamic acid, N-hydroxypeptide and thiol functional groups
Streptomyces metalloproteinase inhibitor
-
i.e. SMPI, molecular dynamics study of enzyme-inhibitor complex. Inhibitor interacts with pseudolysin via the rigid active side loop and several contact sites outside this loop
-
phosphoramidon
N-(alpha-rhamnopyranosyloxyhydroxyphosphinyl)-Leu-Trp
phosphoryl-L-leucyl-L-phenylalanine
at 0.1 mM 98% inhibition with azocasein as substrate, 94% inhibition with elastin as substrate and 98% inhibition with cartilage as substrate, at 0.01 mM 83% inhibition with azocasein as substrate, 87% inhibition with elastin as substrate and 89% inhibition with cartilage as substrate
phosphoramidon
-
N-(alpha-L-rhamnopyranosyloxyhydroxyphosphinyl)-L-leucyl-L-tryptophan
additional information
extracellular elastase activity decreases if cells are cultured in the presence of sub-inhibitory concentrations of certain antibiotics
-
additional information
-
extracellular elastase activity decreases if cells are cultured in the presence of sub-inhibitory concentrations of certain antibiotics
-
additional information
N-alpha mercaptoamide-containing dipeptides as inhibitors
-
additional information
-
N-alpha mercaptoamide-containing dipeptides as inhibitors
-
additional information
-
no inhibition by diisopropylphosphofluoridate at 20 mM
-
additional information
-
no inhibition by dithio-bis(nitrobenzoic acid) and phenylmethylsulfonyl fluoride, and by K+ and Na+
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
no stimulation by ceftazidime and gentamycin
-
additional information
-
no stimulation by ceftazidime and gentamycin
-
additional information
-
the pro-sequence, consisting of 174 amino acids, is cleaved by autoproteolytic processing in the periplasm to produce the active, mature elastase of 301 amino acids
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.4
3-(2-furyl)acryloyl-glycyl-L-phenylalanyl-L-phenylalanine
-
1.8
Benzyloxycarbonyl-Gly-Leu-Ala
-
benzyloxycarbonyl-Gly-Leu-Leu, benzyloxycarbonyl-Phe-Leu-Ala
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
240
3-(2-furyl)acryloyl-glycyl-L-phenylalanyl-L-phenylalanine
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.034
2-mercaptoacetyl-Leu-Dphe
at pH 7.5 and 25°C, with furylacryloyl-glycyl-L-leucyl-L-alanine as substrate
0.0015
2-mercaptoacetyl-Leu-Phe
at pH 7.5 and 25°C, with furylacryloyl-glycyl-L-leucyl-L-alanine as substrate
0.0002
2-mercaptoacetyl-Phe-Leu
at pH 7.5 and 25°C, with furylacryloyl-glycyl-L-leucyl-L-alanine as substrate
0.028
benzyloxycarbonyl-Gly-NHOH
at pH 7.5 and 25°C, with furylacryloyl-glycyl-L-leucyl-L-alanine as substrate
6.2
benzyloxycarbonyl-L-leucine
at pH 7.5 and 25°C, with furylacryloyl-glycyl-L-leucyl-L-alanine as substrate
5
benzyloxycarbonyl-L-phenylalanine
at pH 7.5 and 25°C, with furylacryloyl-glycyl-L-leucyl-L-alanine as substrate
0.011
benzyloxycarbonyl-Leu-NHOH
at pH 7.5 and 25°C, with furylacryloyl-glycyl-L-leucyl-L-alanine as substrate
0.021
benzyloxycarbonyl-Phe-NHOH
at pH 7.5 and 25°C, with furylacryloyl-glycyl-L-leucyl-L-alanine as substrate
1.1
Leu-Phe
at pH 7.5 and 25°C, with furylacryloyl-glycyl-L-leucyl-L-alanine as substrate
0.4
Phe-Leu
at pH 7.5 and 25°C, with furylacryloyl-glycyl-L-leucyl-L-alanine as substrate
0.0002
phosphoryl-L-leucyl-L-phenylalanine
at pH 7.5 and 25°C, with furylacryloyl-glycyl-L-leucyl-L-alanine as substrate
0.0004
rapidly eluting isomer of HSCH2(DL)CH[CH2CH(CH3)2]CO-Phe-Ala-NH2
-
-
0.0003
slowly eluting isomer of HSCH2(DL)CH[CH2CH(CH3)2]CO-Phe-Ala-NH2
-
-
0.000041
N-mercaptoacetyl-Phe-Tyr-amide
-
pH and temperature not specified in the publication
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00273
1-(biphenyl-4-ylmethyl)-3-hydroxy-2-methylpyridine-4(1H)-thione
Pseudomonas aeruginosa
-
pH and temperature not specified in the publication
0.0000059
N-aryl mercaptoacetamide
Pseudomonas aeruginosa
-
pH and temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2389
-
recombinant glycosylated enzyme, pH 7.5, 60°C, substrate casein
2401
-
recombinant nonglycosylated enzyme, pH 7.5, 60°C, substrate casein
3.2
-
purified recombinant enzyme from Escherichia coli expression, pH 8.0, 25°C, substrate N-succinyl-Ala-Ala-Ala-4-nitroanilide
additional information
additional information
-
development and evaluation of a highly sensitive assay based on internally quenched fluorogenic peptide substrates comprising an edans (5-(2-aminoethylamino)-1-naphthalenesulfonic acid) group at the C-terminus and a dabsyl (4-(dimethylamino)azobenzene-4'-sulfonyl chloride) fluorophore at the N-terminus of the peptide chains, overview
additional information
-
chronic wound fluid samples from infected human subjects, pH 7.3
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.8
with 2-aminobenzoyl-Ala-Gly-Leu-Ala-4-nitrobenzylamide as substrate
7.5
additional information
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 50
-
30°C: about 75% of maximal activity, 50°C: about 85% of maximal activity
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
663597, 663600, 663610, 663749, 664157, 664238, 664848, 665153, 665156, 665158, 665159, 665160, 665163, 665182, 665250, 665354, 665463, 666225, 666234, 666263, 666382, 666385, 666533, 689886, 735268, 754837
SwissProt
exhibits greatly reduced amounts of elastolytic activity
SwissProt
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
mutants E141D, E141Q, E141G, H223G, H223E, and H223L
additional information
-
most abundant peptidase found in pseudomonal secretions, which contributes to the invasiveness of Pseudomonas aeruginosa due to its ability to cleave several extracellular matrix proteins and to disrupt the basolateral intercellular functions present in the host tissues
-
additional information
in the sputum of patients infected with Pseudomonas aeruginosa
-
additional information
-
in the sputum of patients infected with Pseudomonas aeruginosa
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
pseudolysin is a Zn2+ metalloprotease of the thermolysin family
physiological function
evolution
malfunction
-
the exosecretome of the LasB-deficient pseudomonal strain PAO1lasBDELTA has limited impact on human vascular cell adherence and viability
physiological function
additional information
physiological function
pseudolysin is the most abundant protease secreted by Pseudomonas aeruginosa and is the major extracellular virulence factor of this opportunistic human pathogen. Pseudolysin destroys human tissues by solubilizing elastin
physiological function
digestion of thrombin by Pseudomonas aeruginosa elastase leads to the release of the C-terminal thrombin-derived peptide FYT21, which inhibits pro-inflammatory responses to several pathogen-associated molecular patterns in vitro and in vivo by preventing toll-like receptor dimerization and subsequent activation of down-stream signalling pathwaysthe enzyme cleaves a C-terminal peptide from human thrombin that inhibits host inflammatory responses
evolution
-
the typical metalloendopeptidases consensus zinc-binding sequence HEXXH and the catalytic residues in the active site are conserved in the A2 elastase
evolution
-
pseudolysin belongs to the thermolysin-like family of metallopeptidases
physiological function
-
elastase B of Pseudomonas aeruginosa stimulates the humoral immune response in larvae of the greater wax moth, Galleria mellonella. The insects exhibit increased antibacterial activity with appearance of antimicrobial peptides and a higher level of lysozyme in cell-free hemolymph
physiological function
-
Pseudomonal LasB cleaves extracellular matrix proteins involved in adherence of vascular stromal cells in human host. LasB can induce vascular cell anoikis in human cells through simultaneous proteolysis of extracellular matrix components and cell receptors, suggesting the uPAR-vitronectin axis as a major target in this process. In heart valves of patients occurs extensive, LasB-dependent degradation of extracellular matrix-associated fibronectin and vitronectin, that preceeds cell de-adherence, whereas type I collagen shows limited degradation. Disruption of cell/ECM interactions resulting from uncontrolled pericellular proteolysis leads to detachment-induced cell apoptosis, anoikis, contributing to the morbid evolution of inflammatory vascular diseases, overview
physiological function
-
the protease is a virulence factor that acts by destroying peptides of the native immune system
physiological function
-
the enzyme is produced during the course of clinical infections and plays an important role in the virulence of Pseudomonas aeruginosa in chronic lung infections
physiological function
-
the enzyme outstands as a pivotal virulence attribute during the infectious process, playing multifunctional roles in different aspects of the pathogen-host interaction. Most abundant peptidase found in pseudomonal secretions, which contributes to the invasiveness of Pseudomonas aeruginosa due to its ability to cleave several extracellular matrix proteins and to disrupt the basolateral intercellular functions present in the host tissues. Pseudolysin makes Pseudomonas aeruginosa able to overcome host defenses by the hydrolysis of many immunologically relevant molecules, including antibodies and complement components
additional information
mechanism of action of endopeptidase pseudolysin on elastin binding and degradation, pseudolysin has a preference for aromatic and/or large aliphatic amino acids at the P1' position and a distinct bias against acidic residues at the P2' position, overview
additional information
-
mechanism of action of endopeptidase pseudolysin on elastin binding and degradation, pseudolysin has a preference for aromatic and/or large aliphatic amino acids at the P1' position and a distinct bias against acidic residues at the P2' position, overview
additional information
-
the N-terminal signal peptide consists of 23 residues bordered with the signal peptidase recognition site Ala-Phe-Ala-Ala
additional information
-
salt bidges in the enzyme, structure overview. Relationship between salt bridges and stability/enzymatic activity, structure analysis and molecular dynamics using crystal structure with PDB ID 1EZM, overview
additional information
-
the enzyme is synthesized in the cytoplasm as a pre-proenzyme consisting of a 2.4-kDa signal peptid, an 18.1-kDa pro-peptide and the 33.1-kDa mature protein. The signal peptide is cleaved from the pre-proenzyme during translocation across the inner membrane, leaving a 51.2-kDa proenzyme (consisting of the pro-peptide and the mature protein). In the periplasm, the proenzymeis folded, guided by the pro-peptide, and a disulfide bond between Cys270 and Cys297 is formed. The pro-peptide is then removed by autoproteolysis, but remains non-covalently attached to mature pseudolysin. A second disulfide bond between Cys30 and Cys58 of the enzyme is then formed. The pro-peptide and mature enzyme are secreted from the cell together, where they dissociate, and the liberated pro-peptide is degraded by the active enzyme
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
33000
36000
51000
52000
x * 52000, SDS-PAGE, pro-elastase, enzymatically inactive
53600
33000
33030
-
x * 34000, SDS-PAGE, x * 53610, pro-enzyme, sequence calculation, x * 33030, mature enzyme, sequence calculation
34000
-
x * 34000, SDS-PAGE, x * 53610, pro-enzyme, sequence calculation, x * 33030, mature enzyme, sequence calculation
53610
-
x * 34000, SDS-PAGE, x * 53610, pro-enzyme, sequence calculation, x * 33030, mature enzyme, sequence calculation
33000
-
x * 33000, SDS-PAGE, recombinant protein from Escherichia coli
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
?
-
x * 34000, SDS-PAGE, x * 53610, pro-enzyme, sequence calculation, x * 33030, mature enzyme, sequence calculation
additional information
comparison of the 3D structures of PAE and Vibrio cholerae zinc-containing and calcium-stabilized soluble hemagglutinin/protease, HA/P, i.e. vibriolysin, reveals a remarkable similarity having a conserved alpha + beta domain, modelling, overview
additional information
-
comparison of the 3D structures of PAE and Vibrio cholerae zinc-containing and calcium-stabilized soluble hemagglutinin/protease, HA/P, i.e. vibriolysin, reveals a remarkable similarity having a conserved alpha + beta domain, modelling, overview
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
-
the recombinant elastase contains three potential N-glycosylation sites N43, N212, and N280 (Asn-Xaa-Ser/Thr consensus sequences), potential role of N-glycosylation in the activity and stability. Non- and glycosylated isoforms of rPAE display similar kinetic parameters for hydrolyzing casein in aqueous medium, and when catalyzing bipeptide synthesis in 50% v/v DMSO, they exhibit identical substrate specificity and activity, and produce similar yields. The N-linked oligosaccharides of Pichia pastoris-secreted glycoproteins are a high-mannose type (Man8GlcNAc2 or Man9GlcNAc2) with molecular weights close to 2 kDa
proteolytic modification
proteolytic modification
-
the pro-sequence, consisting of 174 amino acids, is cleaved by autoproteolytic processing in the periplasm to produce the active, mature elastase of 301 amino acids
proteolytic modification
-
the enzyme is synthesized in the cytoplasm as a pre-proenzyme consisting of a 2.4-kDa signal peptid, an 18.1-kDa pro-peptide and the 33.1-kDa mature protein. The signal peptide is cleaved from the pre-proenzyme during translocation across the inner membrane, leaving a 51.2-kDa proenzyme (consisting of the pro-peptide and the mature protein). In the periplasm, the proenzymeis folded, guided by the pro-peptide, and a disulfide bond between Cys270 and Cys297 is formed. The pro-peptide is then removed by autoproteolysis, but remains non-covalently attached to mature pseudolysin. A second disulfide bond between Cys30 and Cys58 of the enzyme is then formed. The pro-peptide and mature enzyme are secreted from the cell together, where they dissociate, and the liberated pro-peptide is degraded by the active enzyme
proteolytic modification
LasB is produced as a precursor protein that requires autocatalytic processing to ensure proper folding as it is exported across the outer membrane. Ca2+ is needed either for efficient transcription of lasB or during the process of folding and export, as calcium plays a role in the structural integrity of LasB
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in the presence of inhibitors S-homoPhe [N-alpha-alpha]Phe-IsoAsn, phosphoramidon, and ClCH2CO-HOLeu-Ala-Gly-NH2
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D189A
-
site-directed mutagenesis, the mutant shows decreased thermal stabilities and increased activities compared to the wild-type enzyme
D201A
-
site-directed mutagenesis, the mutant shows slightly increased thermal stability and slightly decreased activity compared to the wild-type enzyme
E249A
-
site-directed mutagenesis, the mutant shows both decreased thermal stability and decreased activity compared to the wild-type enzyme
N212Q
-
site-directed mutagenesis, the mutant enzyme shows similar activity and slightly decreased thermostability compared to the wild-type enzyme
N212Q/N280Q
-
site-directed mutagenesis, 90.6% decreased activity compared to the wild-type enzyme
N280Q
-
site-directed mutagenesis, the mutant enzyme shows similar activity and slightly decreased thermostability compared to the wild-type enzyme
N43Q
-
site-directed mutagenesis, the mutant enzyme shows similar activity and slightly decreased thermostability compared to the wild-type enzyme
N43Q/N212Q
-
site-directed mutagenesis, 68.7% decreased activity compared to the wild-type enzyme
N43Q/N212Q/N280Q
-
site-directed mutagenesis, 90.6% decreased activity compared to the wild-type enzyme
N43Q/N280Q
-
site-directed mutagenesis, 73.6% decreased activity compared to the wild-type enzyme
R179A
-
site-directed mutagenesis, the mutant shows decreased thermal stabilities and increased activities compared to the wild-type enzyme
R205A
-
site-directed mutagenesis, the mutant shows slightly increased thermal stability and slightly decreased activity compared to the wild-type enzyme
additional information
-
mutation of any potential N-glycosylation site was detrimental to its expression in Pichia pastoris with 23.9% decrease in expression of the N43Q mutant, 63.6% of the N212Q mutant, and 63.7% of the N280Q mutant compared with the wild type
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 11
-
purified enzyme, 60 min, loss of 30% activity at pH 5.0 and of 50% at pH 11.0, completely stable at pH 6.0-10.0, profile overview
717673
6 - 9
6 - 9.5
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 60
60
70
30 - 60
-
purified enzyme, completely stable at 30°C and 40°C after 60 min, A2 protease retains about 80% and 60% of its initial activity after incubation for 60 min at 50°C and 60°C, respectively
70
-
half-lives of the glycosylated and non-glycosylated forms of recombinant enzyme are 32.2 and 23.1 min, respectively
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
the first and second disulfide bonds are essential for the stability and activity of the enzyme, respectively
-
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
chloroform
-
pH 7.0, 30°C, 4 days, 95.6% activity remaining for the nonglycosylated recombinant enzyme, 91.5% for the glycosylated recombinant enzyme
DMSO
-
pH 7.0, 30°C, 4 days, 95.1% activity remaining for the nonglycosylated recombinant enzyme, 83.2% for the glycosylated recombinant enzyme
Ethanol
isopropanol
-
pH 7.0, 30°C, 4 days, 39.2% activity remaining for the nonglycosylated recombinant enzyme, 17.5% for the glycosylated recombinant enzyme
Methanol
-
pH 7.0, 30°C, 4 days, 102% activity remaining for the nonglycosylated recombinant enzyme, 96.5% for the glycosylated recombinant enzyme
n-Butanol
-
pH 7.0, 30°C, 4 days, 89.5% activity remaining for the nonglycosylated recombinant enzyme, 78.5% for the glycosylated recombinant enzyme
additional information
-
the enzyme is stable in the presence of organic solvents mainly diethyl ether and DMSO
Ethanol
-
pH 7.0, 30°C, 4 days, 71.5% activity remaining for the nonglycosylated recombinant enzyme, 62.1% for the glycosylated recombinant enzyme
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 0.02 M Tris-hydrochloride, 0.5 mM CaCl2 (pH 7.5), 1 year, less than 10% loss of activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native enzyme 2.23fold to homogeneity by ultrafiltration, gel filtration, and anion exchange chromatography
-
native extracellular enzyme from cell culture medium by ammonium sulfate fractionation, dialysis, anion exchange chromatography, and cation exchange chromatography
-
recombinant wild-type and mutant enzymes from Escherichia coli strain BL21 (DE3) by ammonium sulfate fractionation, anion exchange chromatography
-
solubilized recombinant His-tagged enzyme from Escherichia coli cells by metal affinity chromatography, or the enzyme is simultaneously further purified, refolded and buffer-exchanged on a preparative Superdex 200 column by a modified urea reverse-gradient gel filtration
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expression of mutants E141D, E141Q, E141G, H223G, H223E, and H223L in Escherichia coli JM109
expression in Escherichia coli
gene lasB, recombinant expression in Escherichia coli and in Pichia pastoris and secretion of the enzyme, large-scale expression of His-tagged enzyme under the control of the T7 promoter in Escherichia coli strain BL21(DE3) in inclusion bodies
-
recombinant enzyme expression in Pichia pastoris with heterogeneous N-glycosylation, expression of enzyme glycosylation site mutants
-
recombinant expression of wild-type and mutant enzymes in Escherichia coli strain BL21 (DE3)
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
it is possible that the induction of LasB production is increased by the combined regulatory activities of the Las and Rhl systems in a manner not applicable to AprA
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
solubilization of recombinant His-tagged enzyme from strain BL21(DE3) in inclusion bodies by 8 M urea
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
biotechnology
-
A2 protease is usable for shrimp waste deproteinization in the process of chitin preparation, percent of protein removal after 3 h hydrolysis at 40°C with an enzyme/substrate ratio of 5 U/mg protein is about 75%. A2 proteolytic preparation also demonstrates powerful depilating capabilities of hair removal from bovine skin
diagnostics
-
specific protease activity of the enzyme as indicator for the degree of Pseudomonas aeruginosa infection in chronic infected wounds
industry
medicine
pharmacology
-
branched antimicrobial peptide M33 pegylation at the C-terminus of the three lysine-branching core with a Peg4 molecule and the resulting increase in stability to Pseudomonas aeruginosa elastase, peptide resistance to this protease is an important feature for M33-Peg activity against Pseudomonas aeruginosa
synthesis
-
the Pseudomonas aeruginosa elastase, produced by Pichia pastoris, is a promising biocatalyst for peptide synthesis in organic solvents
medicine
2-mercaptoacetyl-L-phenylalanyl-L-leucine represents a class of potent elastase inhibitors that might prove useful in the management of Pseudomonas aeruginosa infections
medicine
application of the inhibitors may be helpful in the management of corneal infections with Pseudomonas aeruginosa
medicine
Inflammation and consequent lung dysfunction are hallmarks of recurrent Pseudomonas aeruginosa infections in cystic fibrosis lungs. The continued presence of bacterial components, including PE, can evoke an ongoing host inflammatory response by induction of inflammatory cytokinines and chemokinines such as interleukin-8. Although this cytokinine is essential for an effective host defense, continuous neutrophil transmigration and degranulation will damage the lung tissue through neutrophil-derived proteases. Therefore, the use of specific antibody against Pseudomonas elastase as adjuvant therapy along with antibacterial agents can prove an effective approach in the treatment of chronic Pseudomonas aeruginosa infection.
medicine
the inhibitor may have a therapeutic application by delaying the progression of corneal destruction in Pseudomonas keratitis
medicine
the protective activity of elastase mutants against Pseudomonas infections may be useful in producing vaccines
industry
-
A2 protease is usable for shrimp waste deproteinization in the process of chitin preparation, percent of protein removal after 3 h hydrolysis at 40°C with an enzyme/substrate ratio of 5 U/mg protein is about 75%. A2 proteolytic preparation also demonstrates powerful depilating capabilities of hair removal from bovine skin
industry
-
pseudolysin is a biotechnologically important enzyme in the tanning industry
industry
potential application in the leather industry and as a therapeutic agent
medicine
-
phosphoramidon, the inhibitor of the enzyme, may prove beneficial in the treatment of Pseudomonas aeruginosa corneal infections
medicine
-
the inhibitor of the enzyme, 2-mercaptoacetyl-L-phenyalanyl-L-leucine, has therapeutic potential as an adjunct to antibiotics treatment of Pseudomonas keratitis in rabbits
medicine
enzyme can silence the function of proteinase-activated receptor-2 in the respiratory tract, thereby altering the host innate defense mechanisms and respiratory functions, and thus contributing to the setting of a disease like cystic fibrosis
medicine
-
Pseudomonas aeruginosa cytotoxic elastase is enhanced in the presence of the filamentous fungi Aspergillus fumigatus, suggesting that this may have a role to play in the damaging pathology associated with the lung tissue in this disease. This indicates that patients who have a co-colonisation with these two organisms may have a poorer prognosis
medicine
-
the enzyme is a promising target for the development of new anti-virulence compounds
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Nishino, N.; Powers, J.C.
Pseudomonas aeruginosa elastase. Development of a new substrate, inhibitors, and an affinity ligand
J. Biol. Chem.
255
3482-3486
1980
Pseudomonas aeruginosa
Morihara, K.; Tsuzuki, H.
Pseudomonas aeruginosa elastase. Affinity chromatography and some properties as a metalloneutral proteinase
Agric. Biol. Chem.
39
1123-1128
1975
Pseudomonas aeruginosa
-
Morihara, K.
Pseudolysin and other pathogen endopeptidases of thermolysin family
Methods Enzymol.
248
242-253
1995
Pseudomonas aeruginosa, Vibrio cholerae serotype O1
Bever, R.A.; Iglewski, B.H.
Molecular characterization and nucleotide sequence of the Pseudomonas aeruginosa elastase structural gene
J. Bacteriol.
170
4309-4314
1988
Pseudomonas aeruginosa
Kessler, E.; Safrin, M.; Gustin, J.K.; Ohman, D.E.
Elastase and the LasA protease of Pseudomonas aeruginosa are secreted with their propeptides
J. Biol. Chem.
273
30225-30231
1998
Pseudomonas aeruginosa
Mariencheck, W.I.; Alcorn, J.F.; Palmer, S.M.; Wright, J.R.
Pseudomonas aeruginosa elastase degrades surfactant proteins A and D
Am. J. Respir. Cell Mol. Biol.
28
528-537
2003
Pseudomonas aeruginosa (P14756), Pseudomonas aeruginosa
Dulon, S.; Leduc, D.; Cottrell, G.S.; D'Alayer, J.; Hansen, K.K.; Bunnett, N.W.; Hollenberg, M.D.; Pidard, D.; Chignard, M.
Pseudomonas aeruginosa elastase disables proteinase-activated receptor 2 in respiratory epithelial cells
Am. J. Respir. Cell Mol. Biol.
32
411-419
2005
Pseudomonas aeruginosa, Pseudomonas aeruginosa (P14756)
Besson, C.; Saulnier, J.; Wallach, J.M.
Synthetic peptide substrates for a conductimetric assay of Pseudomonas aeruginosa elastase
Anal. Biochem.
237
216-223
1996
Pseudomonas aeruginosa (P14756), Pseudomonas aeruginosa
Burns, F.R.; Paterson, C.A.; Gray, R.D.; Wells, J.T.
Inhibition of Pseudomonas aeruginosa elastase and Pseudomonas keratitis using a thiol-based peptide
Antimicrob. Agents Chemother.
34
2065-2069
1990
Pseudomonas aeruginosa (P14756), Pseudomonas aeruginosa
Poncz, L.
Substrate inhibition of Pseudomonas aeruginosa elastase by 3-(2-furyl)acryloyl-glycyl-L-phenylalanyl-L-phenylalanine
Arch. Biochem. Biophys.
266
508-515
1988
Pseudomonas aeruginosa (P14756), Pseudomonas aeruginosa
Padrines, M.; Bieth, J.G.
Oxidized and Met358-->Leu mutated alpha 1-proteinase inhibitor as substrates of Pseudomonas aeruginosa elastase
Biochim. Biophys. Acta
1163
61-66
1993
Pseudomonas aeruginosa (P14756), Pseudomonas aeruginosa
Saulnier, J.M.; Curtil, F.M.; Duclos, M.C.; Wallach, J.M.
Elastolytic activity of Pseudomonas aeruginosa elastase
Biochim. Biophys. Acta
995
285-290
1989
Pseudomonas aeruginosa (P14756), Pseudomonas aeruginosa
Kocabiyik, S.; Ergin, E.; Turkoglu, S.
Effects of metals on elastase from Pseudomonas aeruginosa SES-938-1
Biol. Trace Elem. Res.
50
25-31
1995
Pseudomonas aeruginosa, Pseudomonas aeruginosa SES-938-1
Kessler, E.; Spierer, A.
Inhibition by phosphoramidon of Pseudomonas aeruginosa elastase injected intracorneally in rabbit eyes
Curr. Eye Res.
3
1075-1078
1984
Pseudomonas aeruginosa
Spierer, A.; Kessler, E.
The effect of 2-mercaptoacetyl-L-phenylalanyl-L-leucine, a specific inhibitor of Pseudomonas aeruginosa elastase, on experimental Pseudomonas keratitis in rabbit eyes
Curr. Eye Res.
3
645-650
1984
Pseudomonas aeruginosa
Jones, A.; Elphick, H.; Pettitt, E.; Everard, M.L.; Evans, G.S.
Colistin stimulates the activity of neutrophil elastase and Pseudomonas aeruginosa elastase
Eur. Respir. J.
19
1136-1141
2002
Pseudomonas aeruginosa (P14756), Pseudomonas aeruginosa
Morihara, K.; Tsuzuki, H.; Oda, K.
Protease and elastase of Pseudomonas aeruginosa: inactivation of human plasma alpha 1-proteinase inhibitor
Infect. Immun.
24
188-193
1979
Pseudomonas aeruginosa (P14756)
Kessler, E.; Israel, M.; Landshman, N.; Chechick, A.; Blumberg, S.
In vitro inhibition of Pseudomonas aeruginosa elastase by metal-chelating peptide derivatives
Infect. Immun.
38
716-723
1982
Pseudomonas aeruginosa (P14756), Pseudomonas aeruginosa
Heck, L.W.; Morihara, K.; McRae, W.B.; Miller, E.J.
Specific cleavage of human type III and IV collagens by Pseudomonas aeruginosa elastase
Infect. Immun.
51
115-118
1986
Pseudomonas aeruginosa (P14756), Pseudomonas aeruginosa
Poncz, L.; Jentoft, N.; Ho, M.C.; Dearborn, D.G.
Kinetics of proteolysis of hog gastric mucin by human neutrophil elastase and by Pseudomonas aeruginosa elastase
Infect. Immun.
56
703-704
1988
Pseudomonas aeruginosa (P14756), Pseudomonas aeruginosa
Bejarano, P.A.; Langeveld, J.P.; Hudson, B.G.; Noelken, M.E.
Degradation of basement membranes by Pseudomonas aeruginosa elastase
Infect. Immun.
57
3783-3787
1989
Pseudomonas aeruginosa (P14756), Pseudomonas aeruginosa
Hse, C.C.; Finkelstein, R.A.
Comparison of the Vibrio cholerae hemagglutinin/protease and the Pseudomonas aeruginosa elastase
Infect. Immun.
58
4011-4015
1990
Pseudomonas aeruginosa (P14756), Pseudomonas aeruginosa
Kawamoto, S.; Shibano, Y.; Fukushima, J.; Ishii, N.; Morihara, K.; Okuda, K.
Site-directed mutagenesis of Glu-141 and His-223 in Pseudomonas aeruginosa elastase: catalytic activity, processing, and protective activity of the elastase against Pseudomonas infection
Infect. Immun.
61
1400-1405
1993
Pseudomonas aeruginosa (P14756), Pseudomonas aeruginosa
Wolz, C.; Hohloch, K.; Ocaktan, A.; Poole, K.; Evans, R.W.; Rochel, N.; Albrecht-Gary, A.M.; Abdallah, M.A.; Doring, G.
Iron release from transferrin by pyoverdin and elastase from Pseudomonas aeruginosa
Infect. Immun.
62
4021-4027
1994
Pseudomonas aeruginosa (P14756)
Azghani, A.O.; Baker, J.W.; Shetty, S.; Miller, E.J.; Bhat, G.J.
Pseudomonas aeruginosa elastase stimulates ERK signaling pathway and enhances IL-8 production by alveolar epithelial cells in culture
Inflamm. Res.
51
506-510
2002
Pseudomonas aeruginosa (P14756), Pseudomonas aeruginosa
Kessler, E.; Kennah, H.E.; Brown, S.I.
Pseudomonas protease. Purification, partial characterization, and its effect on collagen, proteoglycan, and rabbit corneas
Invest. Ophthalmol. Vis. Sci.
16
488-497
1977
Pseudomonas aeruginosa
Kessler, E.; Spierer, A.; Blumberg, S.
Specific inhibition of Pseudomonas aeruginosa elastase injected intracorneally in rabbit eyes
Invest. Ophthalmol. Vis. Sci.
24
1093-1097
1983
Pseudomonas aeruginosa (P14756), Pseudomonas aeruginosa
Marquart, M.E.; Caballero, A.R.; Chomnawang, M.; Thibodeaux, B.A.; Twining, S.S.; O'Callaghan, R.J.
Identification of a novel secreted protease from Pseudomonas aeruginosa that causes corneal erosions
Invest. Ophthalmol. Vis. Sci.
46
3761-3768
2005
Pseudomonas aeruginosa (P14756), Pseudomonas aeruginosa (Q5XPI6), Pseudomonas aeruginosa, Pseudomonas aeruginosa PA103 (Q5XPI6)
Fukushima, J.; Yamamoto, S.; Morihara, K.; Atsumi, Y.; Takeuchi, H.; Kawamoto, S.; Okuda, K.
Structural gene and complete amino acid sequence of Pseudomonas aeruginosa IFO 3455 elastase
J. Bacteriol.
171
1698-1704
1989
Pseudomonas aeruginosa, Pseudomonas aeruginosa IFO3455
McIver, K.; Kessler, E.; Ohman, D.E.
Substitution of active-site His-223 in Pseudomonas aeruginosa elastase and expression of the mutated lasB alleles in Escherichia coli show evidence for autoproteolytic processing of proelastase
J. Bacteriol.
173
7781-7789
1991
Pseudomonas aeruginosa (P14756), Pseudomonas aeruginosa
McIver, K.S.; Olson, J.C.; Ohman, D.E.
Pseudomonas aeruginosa lasB1 mutants produce an elastase, substituted at active-site His-223, that is defective in activity, processing, and secretion
J. Bacteriol.
175
4008-4015
1993
Pseudomonas aeruginosa (P14756)
Thayer, M.M.; Flaherty, K.M.; McKay, D.B.
Three-dimensional structure of the elastase of Pseudomonas aeruginosa at 1.5-A resolution
J. Biol. Chem.
266
2864-2871
1991
Pseudomonas aeruginosa (P14756), Pseudomonas aeruginosa
Kessler, E.; Safrin, M.
The propeptide of Pseudomonas aeruginosa elastase acts an elastase inhibitor
J. Biol. Chem.
269
22726-22731
1994
Pseudomonas aeruginosa (P14756), Pseudomonas aeruginosa
Heck, L.W.; Alarcon, P.G.; Kulhavy, R.M.; Morihara, K.; Russell, M.W.; Mestecky, J.F.
Degradation of IgA proteins by Pseudomonas aeruginosa elastase
J. Immunol.
144
2253-2257
1990
Pseudomonas aeruginosa, Pseudomonas aeruginosa IFO 3455
Azghani, A.O.; Bedinghaus, T.; Klein, R.
Detection of elastase from Pseudomonas aeruginosa in sputum and its potential role in epithelial cell permeability
Lung
178
181-189
2000
Pseudomonas aeruginosa (P14756), Pseudomonas aeruginosa
McKay, D.B.; Thayer, M.M.; Flaherty, K.M.; Pley, H.; Benvegnu, D.
Crystallographic structures of the elastase of Pseudomonas aeruginosa
Matrix Suppl.
1
112-115
1992
Pseudomonas aeruginosa (P14756)
Braun, P.; Bitter, W.; Tommassen, J.
Activation of Pseudomonas aeruginosa elastase in Pseudomonas putida by triggering dissociation of the propeptide-enzyme complex
Microbiology
146
2565-2572
2000
Pseudomonas aeruginosa (P14756)
-
Braun, P.; Tommassen, J.; Filloux, A.
Role of the propeptide in folding and secretion of elastase of Pseudomonas aeruginosa
Mol. Microbiol.
19
297-306
1996
Pseudomonas aeruginosa (P14756)
Galloway, D.R.
Pseudomonas aeruginosa elastase and elastolysis revisited: recent developments
Mol. Microbiol.
5
2315-2321
1991
Pseudomonas aeruginosa (P14756), Pseudomonas aeruginosa, Pseudomonas aeruginosa PAO-E64 (P14756)
Barbey-Morel, C.; Perlmutter, D.H.
Effect of pseudomonas elastase on human mononuclear phagocyte alpha 1-antitrypsin expression
Pediatr. Res.
29
133-140
1991
Pseudomonas aeruginosa (P14756), Pseudomonas aeruginosa
Matheson, N.R.; Potempa, J.; Travis, J.
Interaction of a novel form of Pseudomonas aeruginosa alkaline protease (aeruginolysin) with interleukin-6 and interleukin-8
Biol. Chem.
387
911-915
2006
Pseudomonas aeruginosa
Gupta, A.; Roy, I.; Khare, S.K.; Gupta, M.N.
Purification and characterization of a solvent stable protease from Pseudomonas aeruginosa PseA
J. Chromatogr. A
1069
155-161
2005
Pseudomonas aeruginosa
Adekoya, O.A.; Willassen, N.P.; Sylte, I.
Molecular insight into pseudolysin inhibition using the MM-PBSA and LIE methods
J. Struct. Biol.
153
129-144
2006
Pseudomonas aeruginosa
Elston, C.; Wallach, J.; Saulnier, J.
New continuous and specific fluorometric assays for Pseudomonas aeruginosa elastase and LasA protease
Anal. Biochem.
368
87-94
2007
Pseudomonas aeruginosa
Lutfullah, G.; Amin, F.; Khan, Z.; Azhar, N.; Azim, M.K.; Noor, S.; Shoukat, K.
Homology modeling of hemagglutinin/protease [HA/P (vibriolysin)] from Vibrio cholerae: Sequence comparision, residue interactions and molecular mechanism
Protein J.
27
105-114
2008
Pseudomonas aeruginosa (P14756), Pseudomonas aeruginosa
Kida, Y.; Higashimoto, Y.; Inoue, H.; Shimizu, T.; Kuwano, K.
A novel secreted protease from Pseudomonas aeruginosa activates NF-kappaB through protease-activated receptors
Cell. Microbiol.
10
1491-1504
2008
Pseudomonas aeruginosa
Cheng, M.; Takenaka, S.; Aoki, S.; Murakami, S.; Aoki, K.
Purification and characterization of an eggshell membrane decomposing protease from Pseudomonas aeruginosa strain ME-4
J. Biosci. Bioeng.
107
373-378
2009
Pseudomonas aeruginosa, Pseudomonas aeruginosa ME-4
Beaufort, N.; Corvazier, E.; Hervieu, A.; Choqueux, C.; Dussiot, M.; Louedec, L.; Cady, A.; de Bentzmann, S.; Michel, J.B.; Pidard, D.
The thermolysin-like metalloproteinase and virulence factor LasB from pathogenic Pseudomonas aeruginosa induces anoikis of human vascular cells
Cell. Microbiol.
13
1149-1167
2011
Pseudomonas aeruginosa
Ghorbel-Bellaaj, O.; Khaled, H.B.; Bayoudh, A.; Younes, I.; Hmidet, N.; Jellouli, K.; Nasri, M.
Pseudomonas aeruginosa A2 elastase: Purification, characterization and biotechnological applications
Int. J. Biol. Macromol.
50
679-686
2012
Pseudomonas aeruginosa, Pseudomonas aeruginosa A2
Andrejko, M.; Mizerska-Dudka, M.
Elastase B of Pseudomonas aeruginosa stimulates the humoral immune response in the greater wax moth, Galleria mellonella
J. Invertebr. Pathol.
107
16-26
2011
Pseudomonas aeruginosa
Falciani, C.; Lozzi, L.; Scali, S.; Brunetti, J.; Bracci, L.; Pini, A.
Site-specific pegylation of an antimicrobial peptide increases resistance to Pseudomonas aeruginosa elastase
Amino Acids
46
1403-1407
2014
Pseudomonas aeruginosa
Han, M.; Wang, X.; Ding, H.; Jin, M.; Yu, L.; Wang, J.; Yu, X.
The role of N-glycosylation sites in the activity, stability, and expression of the recombinant elastase expressed by Pichia pastoris
Enzyme Microb. Technol.
54
32-37
2014
Pseudomonas aeruginosa
Wildeboer, D.; Hill, K.E.; Jeganathan, F.; Williams, D.W.; Riddell, A.D.; Price, P.E.; Thomas, D.W.; Stephens, P.; Abuknesha, R.A.; Price, R.G.
Specific protease activity indicates the degree of Pseudomonas aeruginosa infection in chronic infected wounds
Eur. J. Clin. Microbiol. Infect. Dis.
31
2183-2189
2012
Pseudomonas aeruginosa
Bian, F.; Yue, S.; Peng, Z.; Zhang, X.; Chen, G.; Yu, J.; Xuan, N.; Bi, Y.
A comprehensive alanine-scanning mutagenesis study reveals roles for salt bridges in the structure and activity of Pseudomonas aeruginosa elastase
PLoS ONE
10
e121108
2015
Pseudomonas aeruginosa
Odunuga, O.; Adekoya, O.; Sylte, I.
High-level expression of pseudolysin, the extracellular elastase of Pseudomonas aeruginosa, in Escherichia coli and its purification
Protein Expr. Purif.
113
79-84
2015
Pseudomonas aeruginosa
Yang, J.; Zhao, H.; Ran, L.; Li, C.; Zhang, X.; Su, H.; Shi, M.; Zhou, B.; Chen, X.; Zhang, Y.
Mechanistic insights into elastin degradation by pseudolysin, the major virulence factor of the opportunistic pathogen Pseudomonas aeruginosa
Sci. Rep.
5
9936
2015
Pseudomonas aeruginosa (P14756), Pseudomonas aeruginosa
Galdino, A.C.M.; de Oliveira, M.P.; Ramalho, T.C.; de Castro, A.A.; Branquinha, M.H.; Santos, A.L.S.
Anti-virulence strategy against the multidrug-resistant bacterial pathogen Pseudomonas aeruginosa pseudolysin (elastase B) as a potential druggable target
Curr. Protein Pept. Sci.
20
471-487
2019
Pseudomonas aeruginosa
Jose, D.; Mohandas, A.; Bright Singh, I.
Bioprocess technology for LasB protease (elastase) production from Pseudomonas aeruginosa MCCB 123
Indian J. Biotechnol.
17
284-289
2018
Pseudomonas aeruginosa (G1EMI7), Pseudomonas aeruginosa MCCB 123 (G1EMI7)
-
Casilag, F.; Lorenz, A.; Krueger, J.; Klawonn, F.; Weiss, S.; Haeussler, S.
The LasB elastase of Pseudomonas aeruginosa acts in concert with alkaline protease AprA to prevent flagellin-mediated immune recognition
Infect. Immun.
84
162-171
2016
Pseudomonas aeruginosa (Q02RJ6), Pseudomonas aeruginosa UCBPP-PA14 (Q02RJ6)
Said, Z.S.A.M.; Arifi, F.A.M.; Salleh, A.B.; Rahman, R.N.Z.R.A.; Leow, A.T.C.; Latip, W.; Ali, M.S.M.
Unravelling protein -organic solvent interaction of organic solvent tolerant elastase from Pseudomonas aeruginosa strain K crystal structure
Int. J. Biol. Macromol.
127
575-584
2019
Pseudomonas aeruginosa (A7LI11)
Kotb, E.; El-Zawahry, Y.; Saleh, G.
Isolation of a putative virulence agent, cytotoxic serine-elastase, from a newly isolated Pseudomonas aeruginosa ZuhP13
J. Biosci.
44
7
2019
Pseudomonas aeruginosa, Pseudomonas aeruginosa ZuhP13
Smith, K.; Rajendran, R.; Kerr, S.; Lappin, D.F.; Mackay, W.G.; Williams, C.; Ramage, G.
Aspergillus fumigatus enhances elastase production in Pseudomonas aeruginosa co-cultures
Med. Mycol.
53
645-655
2015
Pseudomonas aeruginosa
Li, Y.; Bai, F.; Xia, H.; Zhuang, L.; Xu, H.; Jin, Y.; Zhang, X.; Bai, Y.; Qiao, M.
A novel regulator PA5022 (aefA) is involved in swimming motility, biofilm formation and elastase activity of Pseudomonas aeruginosa
Microbiol. Res.
176
14-20
2015
Pseudomonas aeruginosa, Pseudomonas aeruginosa PA68
van der Plas, M.J.; Bhongir, R.K.; Kjellstroem, S.; Siller, H.; Kasetty, G.; Moergelin, M.; Schmidtchen, A.
Pseudomonas aeruginosa elastase cleaves a C-terminal peptide from human thrombin that inhibits host inflammatory responses
Nat. Commun.
7
11567
2016
Pseudomonas aeruginosa (P14756), Pseudomonas aeruginosa
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