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BRENDA support

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

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

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.24 Metalloendopeptidases
                3.4.24.26 pseudolysin

Organism

Organism on EC 3.4.24.26 - pseudolysin

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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene lasB
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Manually annotated by BRENDA team
gene lasB
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Manually annotated by BRENDA team
isolated from marine water in Sfax city, Tunisia, gene lasB
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Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
the PA5022 mutant (with transposon inactivation of PA5022) forms thicker biofilms compared to the PA68 wild-type strain and is impaired in its elastase activity
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Manually annotated by BRENDA team
exhibits greatly reduced amounts of elastolytic activity
SwissProt
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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WP_084338031.1
GenBank
Manually annotated by BRENDA team
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WP_084338031.1
GenBank
Manually annotated by BRENDA team
similar enzyme produced by Vibrio cholerae
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Manually annotated by BRENDA team