3.4.24.26: pseudolysin
This is an abbreviated version!
For detailed information about pseudolysin, go to the full flat file.
Word Map on EC 3.4.24.26
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3.4.24.26
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thermolysin
-
metalloproteinases
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collagenase
-
metalloprotease
-
3.4.24.4
-
elastin
-
gelatinase
-
elastases
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phosphoramidon
-
pseudomonal
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stromelysin
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thermolysin-like
-
metalloendopeptidase
-
medicine
-
thermoproteolyticus
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aureolysin
-
vibriolysin
-
intrastromal
-
industry
-
nutrition
-
biotechnology
-
synthesis
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pharmacology
-
diagnostics
- 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
Reaction
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
A2 elastase, aeruginolysin, ealastase LasB, EC 3.4.24.4, elastase, elastase B, elastolytic metalloproteinase, EPa, LasB, LasB protease, LepA, More, Neutral metalloproteinase, PAE, PASP, PE, PsE, Pseudomonas aeruginosa elastase, Pseudomonas aeruginosa neutral metalloproteinase, Pseudomonas aeruginosa small protease, Pseudomonas elastase, Pseudomonas protease
ECTree
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Substrates Products
Substrates Products on EC 3.4.24.26 - pseudolysin
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REACTION DIAGRAM
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
-
-
-
-
?
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
-
-
?
7-methoxycoumarin-4-yl-acetyl-Arg-Pro-Pro-Gly-Phe-Ser-Ala-Phe-Lys-(2,4-dinitrophenyl)-OH
?
-
-
-
-
?
AAF-7-amido-4-methylcoumarin + H2O
AAF + 7-amino-4-methylcoumarin
-
-
-
-
?
Ac-DEVD-7-amido-4-methylcoumarin + H2O
Ac-DEVD + 7-amino-4-methylcoumarin
-
-
-
-
?
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)
-
-
?
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
-
-
-
-
?
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
-
-
?
eggshell membrane + H2O
Val-Leu-Pro-Pro + (X)-Val-Pro-Pro + Trp + ?
-
-
-
-
?
human gamma-interferon + H2O
fragments of human gamma-interferon
-
-
-
?
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
-
-
-
-
?
monocyte-derived alpha1-antitrypsin + H2O
?
37°C
51-kD polypeptide
-
?
myeloma IgA2-lamda of A2m(2) allotype + H2O
?
-
predominantly polymeric, 37°C
-
-
?
N-chlorosuccinimide-oxidized inhibitor + H2O
?
25°C, pH 7.4, cleavage occurs between Glu354 and Ala355
-
-
?
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
-
-
-
-
?
proteinase-activated receptor 2 + H2O
?
the enzyme cleaves proteinase-activated receptor 2 to remove the extracellular Flag epitope
-
-
?
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
-
-
-
-
?
tear fluid surfactant protein D + H2O
35000 Da fragment of tear fluid surfactant protein D + ?
-
purified elastase degrades tear fluid surfactant protein D in vitro and in vivo
-
-
?
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
-
-
-
-
?
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
-
-
-
?
azocasein + H2O
?
proteolytic activity is 8 to 9fold lower than in the wild-type strain
-
-
?
?
WP_084338031.1
the enzyme can be applied to obtain bioactive soluble peptides from eggshell-membrane
-
-
?
eggshell-membrane + H2O
?
WP_084338031.1
the enzyme can be applied to obtain bioactive soluble peptides from eggshell-membrane
-
-
?
elastase + ?
-
autocatalytically cleaved
-
?
elastase propeptide + H2O
elastase + ?
-
autocatalytically cleaved
-
?
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
-
-
?
?
the enzyme is capable of degrading exogenous flagellin under calcium-replete conditions and prevents flagellin-mediated immune recognition
-
-
?
flagellin + H2O
?
the enzyme is capable of degrading exogenous flagellin under calcium-replete conditions and prevents flagellin-mediated immune recognition
-
-
?
furylacryloyl-Gly + Leu-NH2
-
poor substrate
-
?
furylacryloyl-Gly-Leu-NH2 + H2O
furylacryloyl-Gly + Leu-NH2
pH 7.5, 23-25°C
-
-
?
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
-
-
?
myeloma IgA1-kappa + H2O
?
-
predominantly monomeric, 37°C
-
-
?
myeloma IgA1-kappa + H2O
?
-
predominantly polymeric, 37°C
-
-
?
N-succinyl-L-(Ala)3-p-nitroanilide + H2O
?
-
36°C, pH 7.5
-
-
?
?
-
-
pseudolysin eliminates epitopes recognized by the R5 antibody, while those detected by the G12 antibody remain intact, despite destruction of the nearby major T-cell epitope QPQLPY
-
-
?
additional information
?
-
-
pseudolysin eliminates epitopes recognized by the R5 antibody, while those detected by the G12 antibody remain intact, despite destruction of the nearby major T-cell epitope QPQLPY
-
-
?
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
?
-
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
?
-
-
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
-
-
?
additional information
?
-
-
enzyme prefers Ser at position P1, Lys at P2 and hydropobic amino acids at the P1' and P2' positions
-
-
?
additional information
?
-
-
no substrate: N-succinyl-Ala-Ala-Ala-p-nitroanilide, N-succinyl-Ala-Pro-Ala-p-nitroanilide
-
-
?
additional information
?
-
Pseudomonas aeruginosa ZuhP13
-
the enzyme shows both hemolytic and hemorrhagic activities in vivo
-
-
?