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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Localization
Localization on EC 3.4.24.26 - pseudolysin
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mutants E141D, E141Q, E141G, H223G, H223E, and H223L
additional information
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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
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in the sputum of patients infected with Pseudomonas aeruginosa
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additional information
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in the sputum of patients infected with Pseudomonas aeruginosa
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