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Literature summary for 3.4.24.26 extracted from

  • Falciani, C.; Lozzi, L.; Scali, S.; Brunetti, J.; Bracci, L.; Pini, A.
    Site-specific pegylation of an antimicrobial peptide increases resistance to Pseudomonas aeruginosa elastase (2014), Amino Acids, 46, 1403-1407.
    View publication on PubMed

Application

Application Comment Organism
pharmacology branched antimicrobial peptide M33 pegylation at the C-terminus of the three lysine-branching core with a Peg4 molecule and the resulting increase in stability to Pseudomonas aeruginosa elastase, peptide resistance to this protease is an important feature for M33-Peg activity against Pseudomonas aeruginosa Pseudomonas aeruginosa

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
Elastin + H2O Pseudomonas aeruginosa
-
?
-
?

Organism

Organism UniProt Comment Textmining
Pseudomonas aeruginosa
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Elastin + H2O
-
Pseudomonas aeruginosa ?
-
?

Synonyms

Synonyms Comment Organism
elastase
-
Pseudomonas aeruginosa

General Information

General Information Comment Organism
physiological function the protease is a virulence factor that acts by destroying peptides of the native immune system Pseudomonas aeruginosa