EC Number   |
General Information |
Reference |
|---|
   3.4.24.26 | evolution |
pseudolysin belongs to the thermolysin-like family of metallopeptidases |
735209 |
| 3.4.24.26 | evolution |
pseudolysin is a metalloprotease belonging to the thermolysin (M4) family proteases |
-, 733055 |
| 3.4.24.26 | evolution |
pseudolysin is a Zn2+ metalloprotease of the thermolysin family |
735268 |
| 3.4.24.26 | evolution |
the enzyme is an M4 family metalloprotease |
735037 |
| 3.4.24.26 | evolution |
the typical metalloendopeptidases consensus zinc-binding sequence HEXXH and the catalytic residues in the active site are conserved in the A2 elastase |
-, 717673 |
| 3.4.24.26 | evolution |
thermolysin and pseudolysin belong to subclan MA(E) of peptidases, also known as the Glu-zincins, of the matrix metalloproteinases family of zinc-containing endoproteinases with broad substrate specificity and extracellular matrix components are among the substrates |
733787 |
| 3.4.24.26 | malfunction |
the exosecretome of the LasB-deficient pseudomonal strain PAO1lasBDELTA has limited impact on human vascular cell adherence and viability |
717465 |
| 3.4.24.26 | more |
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 |
735268 |
| 3.4.24.26 | more |
salt bidges in the enzyme, structure overview. Relationship between salt bridges and stability/enzymatic activity, structure analysis and molecular dynamics using crystal structure with PDB ID 1EZM, overview |
735037 |
| 3.4.24.26 | more |
the enzyme is synthesized in the cytoplasm as a pre-proenzyme consisting of a 2.4-kDa signal peptid, an 18.1-kDa pro-peptide and the 33.1-kDa mature protein. The signal peptide is cleaved from the pre-proenzyme during translocation across the inner membrane, leaving a 51.2-kDa proenzyme (consisting of the pro-peptide and the mature protein). In the periplasm, the proenzymeis folded, guided by the pro-peptide, and a disulfide bond between Cys270 and Cys297 is formed. The pro-peptide is then removed by autoproteolysis, but remains non-covalently attached to mature pseudolysin. A second disulfide bond between Cys30 and Cys58 of the enzyme is then formed. The pro-peptide and mature enzyme are secreted from the cell together, where they dissociate, and the liberated pro-peptide is degraded by the active enzyme |
733746 |
