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
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metalloproteinases
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collagenase
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metalloprotease
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3.4.24.4
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elastin
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gelatinase
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elastases
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phosphoramidon
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pseudomonal
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stromelysin
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thermolysin-like
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metalloendopeptidase
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medicine
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thermoproteolyticus
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aureolysin
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vibriolysin
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intrastromal
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industry
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nutrition
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biotechnology
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synthesis
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pharmacology
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diagnostics
- 3.4.24.26
- thermolysin
- metalloproteinases
- collagenase
- metalloprotease
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3.4.24.4
- elastin
- gelatinase
- elastases
- phosphoramidon
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pseudomonal
- stromelysin
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thermolysin-like
- metalloendopeptidase
- medicine
- thermoproteolyticus
- aureolysin
- vibriolysin
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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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Natural Substrates Products on EC 3.4.24.26 - pseudolysin
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REACTION DIAGRAM
human thrombin + H2O
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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
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PAR2 + H2O
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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
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the enzyme is capable of degrading exogenous flagellin under calcium-replete conditions and prevents flagellin-mediated immune recognition
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flagellin + H2O
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the enzyme is capable of degrading exogenous flagellin under calcium-replete conditions and prevents flagellin-mediated immune recognition
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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
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additional information
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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
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additional information
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probably responsible for the tissue destruction observed during pulmonary and corneal infections by the pathogen organism Pseudomonas aeruginosa
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