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Literature summary for 3.4.24.26 extracted from

  • Yang, J.; Zhao, H.; Ran, L.; Li, C.; Zhang, X.; Su, H.; Shi, M.; Zhou, B.; Chen, X.; Zhang, Y.
    Mechanistic insights into elastin degradation by pseudolysin, the major virulence factor of the opportunistic pathogen Pseudomonas aeruginosa (2015), Sci. Rep., 5, 9936.
    View publication on PubMedView publication on EuropePMC

Inhibitors

Inhibitors Comment Organism Structure
additional information N-alpha mercaptoamide-containing dipeptides as inhibitors Pseudomonas aeruginosa
N-(1-carboxy-3-phenylpropyl)-phenylalanyl-alpha-asparagine enzyme binding structure analysis, PDB ID 1U4G. The inhibitor is bound in the S1-S1’ sub-sites of pseudolysin by hydrogen bonding and hydrophobic and weak van der Waal's interactions Pseudomonas aeruginosa

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ a zinc metalloprotease Pseudomonas aeruginosa

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Pseudomonas aeruginosa P14756
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Elastin + H2O human tropoelastin Pseudomonas aeruginosa ?
-
?
Elastin + H2O pseudolysin bound to bovine elastin fibers and preferred to attack peptide bonds with hydrophobic residues at the P1 and P1' positions in the hydrophobic domains of elastin Pseudomonas aeruginosa ?
-
?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
55
-
assay at Pseudomonas aeruginosa

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
additional information
-
an endopeptidase active at neutral pH Pseudomonas aeruginosa
8
-
assay at Pseudomonas aeruginosa

General Information

General Information Comment Organism
evolution pseudolysin is a Zn2+ metalloprotease of the thermolysin family Pseudomonas aeruginosa
additional information mechanism of action of endopeptidase pseudolysin on elastin binding and degradation, pseudolysin has a preference for aromatic and/or large aliphatic amino acids at the P1' position and a distinct bias against acidic residues at the P2' position, overview Pseudomonas aeruginosa
physiological function pseudolysin is the most abundant protease secreted by Pseudomonas aeruginosa and is the major extracellular virulence factor of this opportunistic human pathogen. Pseudolysin destroys human tissues by solubilizing elastin Pseudomonas aeruginosa