Any feedback?
Literature summary for 3.4.23.49 extracted from
- Inhibition of outer membrane proteases of the omptin family by aprotinin (2015), Infect. Immun., 83, 2300-2311 .
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| Escherichia coli lipopolysaccharide | LPS, required for omptin activity | Citrobacter rodentium |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene croP, recombinant expression of wild-type enzyme in DELTAcroP-deletion mutant strain of Citrobacter rodentium | Citrobacter rodentium |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| D210A | site-directed mutagenesis by overlap extension PCR | Citrobacter rodentium |
| H212A | site-directed mutagenesis by overlap extension PCR | Citrobacter rodentium |
| additional information | generation of a Citrobacter rodentium DELTAcroP strain | Citrobacter rodentium |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| Aprotinin | classical protease inhibitors are ineffective against CroP activity, but the serine protease inhibitor aprotinin displays inhibitory potency in the micromolar range. Aprotinin acts as a competitive inhibitor of CroP activity and interferes with the cleavage of the murine cathelicidin-related antimicrobial peptide. Structural model of the aprotinin-omptin complex in which Lys15 of aprotinin forms salt bridges with conserved negatively charged residues of the omptin active site, molecular docking, overview. Aprotinin inhibits CRAMP proteolytic degradation by CroP. Docking model of the aprotinin-omptin complex. Lys15 of aprotinin interacts with Glu27 and Asp208 (OmpT numbering), which are the two negatively charged residues that form the S1 specificity pocket of omptins | Citrobacter rodentium |  |
| Aprotinin | ability of EHEC EDL933 cells to cleave the FRET substrate in the presence of increasing concentrations of aprotinin, about 90% inhibition at 0.2 mM. Docking model of the aprotinin-omptin complex. Lys15 of aprotinin interacts with Glu27 and Asp208 (OmpT numbering), which are the two negatively charged residues that form the S1 specificity pocket of omptin | Escherichia coli | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Citrobacter rodentium | - |
- |
- |
| Escherichia coli | P09169 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant wild-type enzyme CroP from DELTAcroP-deletion mutant strain of Citrobacter rodentium crude extract by detergent solubilization, ultracentrifugation, anion exchange chromatography, and dialysis | Citrobacter rodentium |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| Abz-SLGRKIQIK(Dnp)-NH2 + H2O | - |
Citrobacter rodentium | Abz-SLGR + KIQIK(Dnp)-NH2 | - |
? | |
| cathelicidin-related antimicrobial peptide + H2O | CRAMP, a murine cathelicidin-related antimicrobial peptide | Citrobacter rodentium | ? | - |
? | |
| additional information | purified enzyme CroP readily cleaves both a synthetic fluorescence resonance energy transfer substrate and the murine cathelicidin-related antimicrobial peptide, while it poorly activates plasminogen into active plasmin | Citrobacter rodentium | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 32900, about, mature enzyme, sequence calculation | Citrobacter rodentium |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| CroP | - |
Citrobacter rodentium |
| ompT | - |
Escherichia coli |
| ompT | - |
Citrobacter rodentium |
| outer membrane protease | - |
Escherichia coli |
| outer membrane protease | - |
Citrobacter rodentium |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 22 | - |
assay at room temperature | Citrobacter rodentium |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7 | - |
- |
Citrobacter rodentium |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 6 | 8 | CroP exhibits robust activity over a pH range of 6.0 to 8.0, with optimal activity at pH 7.0 | Citrobacter rodentium |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | the enzyme belongs to the omptin family of enzymes | Escherichia coli |
| evolution | the enzyme belongs to the omptin family of enzymes | Citrobacter rodentium |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
