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 | Comment | Organism | Structure |
---|---|---|---|
Zn2+ | a zinc metalloprotease | Pseudomonas aeruginosa |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
Elastin + H2O | Pseudomonas aeruginosa | human tropoelastin | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Pseudomonas aeruginosa | P14756 | - |
- |
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 Maximum [°C] | Comment | Organism |
---|---|---|---|
55 | - |
assay at | Pseudomonas aeruginosa |
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 | 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 |