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Literature summary extracted from

  • Peters, J.E.; Park, S.J.; Darzins, A.; Freck, L.C.; Saulnier, J.M.; Wallach, J.M.; Galloway, D.R.
    Further studies on Pseudomonas aeruginosa LasA: analysis of specificity (1992), Mol. Microbiol., 6, 1155-1162.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.24.B16 additional information no inhibition by EDTA and o-phenanthroline Pseudomonas aeruginosa
3.4.24.B16 N-tosyl-L-lysine chloromethyl ketone
-
Pseudomonas aeruginosa
3.4.24.B16 Phenylmethylsulfonylfluoride
-
Pseudomonas aeruginosa

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.4.24.B16 extracellular active fragment Pseudomonas aeruginosa
-
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.4.24.B16 additional information enzyme is no metalloprotease Pseudomonas aeruginosa

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.4.24.B16 protein + H2O Pseudomonas aeruginosa
-
peptides
-
?

Organism

EC Number Organism UniProt Comment Textmining
3.4.24.B16 Pseudomonas aeruginosa
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
3.4.24.B16 proteolytic degradation of proteins enzyme might be a modified serine protease with a His residue in the active site, specifically involved in degradation of elastin Pseudomonas aeruginosa

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.24.B16 beta-casein + H2O only 1 cleavage site: in the sequence NKKIEKFQphosphorylated-S between Lys and Ile, serine protease activity Pseudomonas aeruginosa beta-casein + 30 amino acid residues fragment
-
?
3.4.24.B16 Elastin + H2O 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 Pseudomonas aeruginosa ?
-
?
3.4.24.B16 additional information 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 Pseudomonas aeruginosa ?
-
?
3.4.24.B16 protein + H2O
-
Pseudomonas aeruginosa peptides
-
?

Synonyms

EC Number Synonyms Comment Organism
3.4.24.B16 LasA
-
Pseudomonas aeruginosa
3.4.24.B16 M23.002 Merops-ID Pseudomonas aeruginosa
3.4.24.B16 staphylolysin
-
Pseudomonas aeruginosa