General Stability | Organism |
---|---|
rapid freezing and thawing inactivates | Escherichia coli |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
diisopropyl fluorophosphate | 10 mM, about 70% inhibition | Escherichia coli | |
dithiothreitol | - |
Escherichia coli | |
NEM | preincubation with followed by inactivation of dithiothreitol causes inhibition of peptide hydrolysis | Escherichia coli | |
phenylmethylsulfonyl fluoride | 2 mM, about 70% inhibition | Escherichia coli |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
19000 | - |
x * 19000, HslV protein, SDS-PAGE | Escherichia coli |
250000 | - |
purified HslV in presence or absence of ATP, gel filtration | Escherichia coli |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Purification (Comment) | Organism |
---|---|
- |
Escherichia coli |
Storage Stability | Organism |
---|---|
-70°C, stable for at least 1 month in presence of 20% glycerol and 1 mM dithiothreitol | Escherichia coli |
4°C rapid inactivation in absence of dithiothreitol | Escherichia coli |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
benzyloxycarbonyl-GGL-7-amido-4-methylcoumarin + H2O | HslV alone cleaves to a much lesser extent than in presence of HslU | Escherichia coli | benzyloxycarbonyl-GGL + 7-amino-4-methylcoumarin | - |
? | |
additional information | HslV and HslU can function together as a novel ATP-dependent protease, the HslVU protease. Pure HslV is a weak peptidase degrading certain hydrophobic peptides. HslU dramatically stimulates peptide hydrolysis by HslV when ATP is present. With a 1:4 molar ratio of HslV to HslU, approximately a 200fold increase in peptide hydrolysis is observed. HslV stimulates the ATPase activity of HslU 2-4fold. CTP and dATP are slowly hydrolyzed by HslU and allow some peptide hydrolysis | Escherichia coli | ? | - |
? | |
succinyl-LLVY-7-amido-4-methylcoumarin + H2O | - |
Escherichia coli | succinyl-LLVY + 7-amino-4-methylcoumarin | - |
? |
Subunits | Comment | Organism |
---|---|---|
? | x * 19000, HslV protein, SDS-PAGE | Escherichia coli |
More | HslVU protease is a two-component protease in which HslV harbors the peptidase activity, while HslU provides an essential ATPase activity | Escherichia coli |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ATP | HslV and HslU can function together as a novel ATP-dependent protease, the HslVU protease. Pure HslV is a weak peptidase degrading certain hydrophobic peptides. HslU dramatically stimulates peptide hydrolysis by HslV when ATP is present. With a 1:4 molar ratio of HslV to HslU, approximately a 200fold increase in peptide hydrolysis is observed. HslV stimulates the ATPase activity of HslU 2-4fold. CTP and dATP are slowly hydrolyzed by HslU and allow some peptide hydrolysis | Escherichia coli |