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Literature summary extracted from
- Substrate specificity of the Escherichia coli outer membrane protease OmpP (2007), J. Bacteriol., 189, 522-530.
Activating Compound
| EC Number | Activating Compound | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.4.23.49 | lipopolysaccharide | OmpT protein active only in the presence of | Escherichia coli |  |
| 3.4.23.49 | lipopolysaccharide | purified OmpP protease active only in the presence of, similar to OmpT protein homologue | Escherichia coli | |
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 3.4.23.49 | expressed in Escherichia coli XL1-Blue, additional strains and plasmids listed, construction of phage libraries and substrate phage described | Escherichia coli |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.4.23.49 | 0.008 | - |
WLARRRGAG | different cleavage sites used by OmpP or OmpT proteases | Escherichia coli | |
| 3.4.23.49 | 0.012 | - |
WLRARRGAG | - |
Escherichia coli | |
| 3.4.23.49 | 0.023 | - |
WEEGGRRIGRGGK | used as a control substrate for determination of the activity of OmpT protease | Escherichia coli | |
| 3.4.23.49 | 0.032 | - |
WLRARRGAG | - |
Escherichia coli | |
| 3.4.23.49 | 0.055 | - |
WEEGGRRIGRGGK | used as a control substrate for determination of the activity of OmpT protease | Escherichia coli | |
| 3.4.23.49 | 0.057 | - |
WLSARRGAG | - |
Escherichia coli | |
| 3.4.23.49 | 0.059 | - |
WLAARRGAG | - |
Escherichia coli | |
| 3.4.23.49 | 0.11 | - |
WLAARRGAG | - |
Escherichia coli | |
| 3.4.23.49 | 0.11 | - |
WLAARRGRG | - |
Escherichia coli | |
| 3.4.23.49 | 0.11 | - |
WLSARRGAG | - |
Escherichia coli | |
| 3.4.23.49 | 0.15 | - |
WLATRRGAG | - |
Escherichia coli | |
| 3.4.23.49 | 0.16 | - |
WLAASRGAG | - |
Escherichia coli | |
| 3.4.23.49 | 0.19 | - |
WLARRRGAG | different cleavage sites used by OmpP or OmpT proteases | Escherichia coli | |
| 3.4.23.49 | 0.216 | - |
WLAAKKGAG | - |
Escherichia coli | |
| 3.4.23.49 | 0.24 | - |
WLSERRGAG | - |
Escherichia coli | |
| 3.4.23.49 | 0.35 | - |
WLAARRGRG | - |
Escherichia coli | |
| 3.4.23.49 | 0.41 | - |
WLAASRGAG | - |
Escherichia coli | |
| 3.4.23.49 | 0.478 | - |
WLAAKKGAG | - |
Escherichia coli | |
| 3.4.23.49 | 0.72 | - |
WLATRRGAG | - |
Escherichia coli | |
| 3.4.23.49 | 0.74 | - |
WLSERRGAG | - |
Escherichia coli | |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 3.4.23.49 | outer membrane | - |
Escherichia coli | 19867 | - |
| 3.4.23.49 | outer membrane | cell surface | Escherichia coli | 19867 | - |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.4.23.49 | Escherichia coli | P09169 | - |
- |
| 3.4.23.49 | Escherichia coli | P34210 | - |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 3.4.23.49 | recombinant protein, gel filtration and SDS-PAGE | Escherichia coli |
Specific Activity [micromol/min/mg]
| EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|---|
| 3.4.23.49 | additional information | - |
phage display applied to analyse substrate specificity of OmpP protease in comparison to OmpT protease, different substrate specificities between OmpP and OmpT proteases determined and discussed as important for inactivation of cationic antimicrobial peptides, cleavage products determined by mass spectrometry, sequence comparison and structural models of OmpP and OmpT proteins shown, effects of ompP and ompT protein on protamine resistance determined | Escherichia coli |
| 3.4.23.49 | additional information | - |
phage display applied to analyse substrate specificity of OmpT protease in comparison to OmpP protease, different substrate specificities between OmpT and OmpP proteases determined and discussed as important for inactivation of cationic antimicrobial peptides, cleavage products determined by mass spectrometry, sequence comparison and structural models of OmpP and OmpT proteins shown, effects of ompP and ompT protein on protamine resistance determined | Escherichia coli |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.4.23.49 | WEEGGRRIGRGGK + H2O | used as a control substrate for determination of the activity of OmpT protease | Escherichia coli | ? | - |
? | |
| 3.4.23.49 | WLAAKKGAG + H2O | differences in substrate specificity between OmpP and OmpT proteases determined | Escherichia coli | ? | - |
? | |
| 3.4.23.49 | WLAAKKGAG + H2O | differences in substrate specificity between OmpT and OmpP proteases determined | Escherichia coli | ? | - |
? | |
| 3.4.23.49 | WLAARRGAG + H2O | differences in substrate specificity between OmpP and OmpT proteases determined | Escherichia coli | ? | - |
? | |
| 3.4.23.49 | WLAARRGAG + H2O | differences in substrate specificity between OmpT and OmpP proteases determined | Escherichia coli | ? | - |
? | |
| 3.4.23.49 | WLAARRGRG + H2O | differences in substrate specificity between OmpP and OmpT proteases determined | Escherichia coli | ? | - |
? | |
| 3.4.23.49 | WLAARRGRG + H2O | differences in substrate specificity between OmpT and OmpP proteases determined | Escherichia coli | ? | - |
? | |
| 3.4.23.49 | WLAASRGAG + H2O | differences in substrate specificity between OmpP and OmpT proteases determined | Escherichia coli | ? | - |
? | |
| 3.4.23.49 | WLAASRGAG + H2O | differences in substrate specificity between OmpT and OmpP proteases determined | Escherichia coli | ? | - |
? | |
| 3.4.23.49 | WLARRRGAG + H2O | different cleavage sites between OmpP and OmpT protease determined | Escherichia coli | ? | - |
? | |
| 3.4.23.49 | WLARRRGAG + H2O | different cleavage sites between OmpT and OmpP protease determined | Escherichia coli | ? | - |
? | |
| 3.4.23.49 | WLATRRGAG + H2O | differences in substrate specificity between OmpP and OmpT proteases determined | Escherichia coli | ? | - |
? | |
| 3.4.23.49 | WLATRRGAG + H2O | differences in substrate specificity between OmpT and OmpP proteases determined | Escherichia coli | ? | - |
? | |
| 3.4.23.49 | WLRARRGAG + H2O | differences in substrate specificity between OmpP and OmpT proteases determined | Escherichia coli | ? | - |
? | |
| 3.4.23.49 | WLRARRGAG + H2O | differences in substrate specificity between OmpT and OmpP proteases determined | Escherichia coli | ? | - |
? | |
| 3.4.23.49 | WLSARRGAG + H2O | differences in substrate specificity between OmpP and OmpT proteases determined | Escherichia coli | ? | - |
? | |
| 3.4.23.49 | WLSARRGAG + H2O | differences in substrate specificity between OmpT and OmpP proteases determined | Escherichia coli | ? | - |
? | |
| 3.4.23.49 | WLSERRGAG + H2O | differences in substrate specificity between OmpP and OmpT proteases determined | Escherichia coli | ? | - |
? | |
| 3.4.23.49 | WLSERRGAG + H2O | differences in substrate specificity between OmpT and OmpP proteases determined | Escherichia coli | ? | - |
? | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.4.23.49 | OmpP protease | F episome-encoded outer membrane protease, 71% amino acid sequence identity with OmpT protease | Escherichia coli |
| 3.4.23.49 | OmpT protease | - |
Escherichia coli |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.4.23.49 | 37 | - |
activity assay at | Escherichia coli |
Turnover Number [1/s]
| EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.4.23.49 | 0.03 | - |
WLAASRGAG | - |
Escherichia coli | |
| 3.4.23.49 | 0.17 | - |
WLAASRGAG | - |
Escherichia coli | |
| 3.4.23.49 | 0.6 | - |
WLSERRGAG | - |
Escherichia coli | |
| 3.4.23.49 | 1.2 | - |
WLAAKKGAG | - |
Escherichia coli | |
| 3.4.23.49 | 1.2 | - |
WLARRRGAG | different cleavage sites used by OmpP or OmpT proteases | Escherichia coli | |
| 3.4.23.49 | 1.5 | - |
WLSERRGAG | - |
Escherichia coli | |
| 3.4.23.49 | 2.2 | - |
WLARRRGAG | different cleavage sites used by OmpP or OmpT proteases | Escherichia coli | |
| 3.4.23.49 | 3.4 | - |
WEEGGRRIGRGGK | used as a control substrate for determination of the activity of OmpT protease | Escherichia coli | |
| 3.4.23.49 | 5 | - |
WLRARRGAG | - |
Escherichia coli | |
| 3.4.23.49 | 5 | - |
WLATRRGAG | - |
Escherichia coli | |
| 3.4.23.49 | 8 | - |
WLAARRGAG | - |
Escherichia coli | |
| 3.4.23.49 | 8.8 | - |
WEEGGRRIGRGGK | used as a control substrate for determination of the activity of OmpT protease | Escherichia coli | |
| 3.4.23.49 | 9 | - |
WLATRRGAG | - |
Escherichia coli | |
| 3.4.23.49 | 13 | - |
WLAARRGAG | - |
Escherichia coli | |
| 3.4.23.49 | 13 | - |
WLAAKKGAG | - |
Escherichia coli | |
| 3.4.23.49 | 37 | - |
WLRARRGAG | - |
Escherichia coli | |
| 3.4.23.49 | 67 | - |
WLSARRGAG | - |
Escherichia coli | |
| 3.4.23.49 | 130 | - |
WLAARRGRG | - |
Escherichia coli | |
| 3.4.23.49 | 168 | - |
WLSARRGAG | - |
Escherichia coli | |
| 3.4.23.49 | 900 | - |
WLAARRGRG | - |
Escherichia coli | |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.4.23.49 | 6.1 | - |
activity assay at | Escherichia coli |
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