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Literature summary extracted from
- Purification, characterization, and primary structure of Escherichia coli protease VII with specificity for paired basic residues: identity of protease VII and OmpT (1988), J. Bacteriol., 170, 5625-5632.
Activating Compound
| EC Number | Activating Compound | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.4.23.49 | 1,10-phenanthroline | enhances activity | Escherichia coli |  |
| 3.4.23.49 | EDTA | enhances activity | Escherichia coli | |
| 3.4.23.49 | tosyl-L-Lys chloromethyl ketone | increases activity | Escherichia coli | |
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 3.4.23.49 | - |
Escherichia coli |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.4.23.49 | Co2+ | - |
Escherichia coli | |
| 3.4.23.49 | Cu2+ | - |
Escherichia coli | |
| 3.4.23.49 | diisopropylfluorophosphate | - |
Escherichia coli | |
| 3.4.23.49 | Fe2+ | - |
Escherichia coli | |
| 3.4.23.49 | tosyl-L-phenylalanine chloromethyl ketone | - |
Escherichia coli | |
| 3.4.23.49 | Zn2+ | - |
Escherichia coli | |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 3.4.23.49 | outer membrane | associated | Escherichia coli | 19867 | - |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 3.4.23.49 | 36000 | - |
x * 36000, SDS-PAGE | Escherichia coli |
| 3.4.23.49 | 180000 | - |
E. coli, gel filtration in presence of Triton X-100 | Escherichia coli |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.4.23.49 | Escherichia coli | - |
- |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 3.4.23.49 | - |
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 | 58.7 | - |
- |
Escherichia coli |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.4.23.49 | alpha-Neo-endorphin + H2O | cleaved at Arg6-Lys7 | Escherichia coli | ? | - |
? | |
| 3.4.23.49 | dynorphin A + H2O | cleavage at Arg6-Arg7 | Escherichia coli | ? | - |
? | |
| 3.4.23.49 | Mastoparan + H2O | cleavage at Lys11-Lys12 | Escherichia coli | ? | - |
? | |
| 3.4.23.49 | additional information | not cleaved: insulin B-chain, parathyroid hormone 13-26 and 26-34, small synthetic substrates e.g. Lys-Lys-Leu-Gln-Asp-Val-His-Asn-Phe | Escherichia coli | ? | - |
? | |
| 3.4.23.49 | additional information | t-butyloxycarbonyl-Leu-Gly-Arg 4-methylcoumarin 7-amide | Escherichia coli | ? | - |
? | |
| 3.4.23.49 | additional information | endopeptidase specifically recognizing and cleaving consecutive basic residues | Escherichia coli | ? | - |
? | |
| 3.4.23.49 | Parathyroid hormone13-34 + H2O | human, cleaved at both Arg25-Lys26 and Lys26-Lys27 | Escherichia coli | ? | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 3.4.23.49 | ? | x * 36000, SDS-PAGE | Escherichia coli |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.4.23.49 | E. coli protease VII | - |
Escherichia coli |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.4.23.49 | 6 | - |
- |
Escherichia coli |
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