3.4.24.B16: protease lasA
This is an abbreviated version!
For detailed information about protease lasA, go to the full flat file.
Word Map on EC 3.4.24.B16
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3.4.24.B16
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aeruginosa
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elastase
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quorum
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pyocyanin
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lysostaphin
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rhamnolipids
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globisporus
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pyoverdine
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sensing-controlled
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pentaglycine
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lyticus
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qs-controlled
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medicine
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degradation
- 3.4.24.B16
- aeruginosa
- elastase
-
quorum
- pyocyanin
- lysostaphin
- rhamnolipids
- globisporus
-
pyoverdine
-
sensing-controlled
- pentaglycine
- lyticus
-
qs-controlled
- medicine
- degradation
Reaction
proteolytic degradation of proteins =
Synonyms
bacteriolytic enzyme, LasA, LasA endopeptidase, LasA protease, M23.002, Pseudomonas elastase, staphylolysin, staphylolytic enzyme
ECTree
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Substrates Products
Substrates Products on EC 3.4.24.B16 - protease lasA
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REACTION DIAGRAM
4-(dimethylamino)azobenzene-4'-sulfonyl chloride-Leu-Gly-Gly-Gly-Ala-5-(2-aminoethylamino)-1-naphthalenesulfonic acid + H2O
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beta-casein + H2O
beta-casein + 30 amino acid residues fragment
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only 1 cleavage site: in the sequence NKKIEKFQphosphorylated-S between Lys and Ile, serine protease activity
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Elastin + H2O
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cleavage of elastin by the enzyme possibly results in the unfolding or disruption of the complex elastin structure, thus providing more access to elastase and other proteases, elastolytic activity in absence of elastase, enzyme also enhances the elastolytic activity of elastase together with alkaline phophatase
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Elastin + H2O
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soluble recombinant and insoluble elastin
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Elastin + H2O
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contributes to the pathogenesis of Pseudomonas aeruginosa
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Elastin + H2O
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enzyme activates elastase, and the elastolytic activity of other proteases by cleaving elastin
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Elastin + H2O
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contributes to the pathogenesis of Pseudomonas aeruginosa
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Leu-4-nitroanilide + succinyl-Gly-Gly
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succinyl-Gly-Gly-Leu-4-nitroanilide + H2O
Leu-4-nitroanilide + succinyl-Gly-Gly
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Phe-4 nitroanilide + succinyl-Gly-Gly
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better substrate than succinyl-Gly-Gly-Leu-4-nitroanilide
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succinyl-Gly-Gly-Phe-4-nitroanilide + H2O
Phe-4 nitroanilide + succinyl-Gly-Gly
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better substrate than succinyl-Gly-Gly-Leu-4-nitroanilide
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enzyme activates elastase, and the elastolytic activity of thermolysin, human neutrophil elastase, proteinase K, by interacting with the elastin substrate rather than the other enzyme
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additional information
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no activity with tosyl-Gly-Pro-Lys-4-nitroanilide, enzyme activates elastase, and the elastolytic, not the proteolytic, activity of thermolysin, human neutrophil elastase, proteinase K, by interacting with the elastin substrate rather than the other enzymes
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additional information
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enzyme specifically promotes growth inhibition and lysis of Staphylococcus aureus cells
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additional information
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enzyme specifically promotes growth inhibition and lysis of Staphylococcus aureus cells
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additional information
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enzyme specifically promotes growth inhibition and lysis of Staphylococcus aureus cells by cleaving the peptidoglycan pentaglycine interpeptides
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additional information
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no cleavage of beta-casein, does not bind chitin
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additional information
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no hydrolysis of 4-(dimethylamino)azobenzene-4'-sulfonyl chloride-Ala-Ala-Phe-Ala-5-(2-aminoethylamino)-1-naphthalenesulfonic acid
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additional information
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staphylolytic activity is pentaglycine in the peptidoglycan of Staphylococcus aureus
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additional information
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enzyme specifically promotes growth inhibition and lysis of Staphylococcus aureus cells
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