Inhibitors | Comment | Organism | Structure |
---|---|---|---|
N-acetyl-Leu-Leu-norleucinal | i.e. calpain inhibitor-I, inhibits HslV | Escherichia coli |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | kinetics, analysis of interaction of free and inhibited HslV with HslU | Escherichia coli |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | - |
Escherichia coli |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
alpha-casein + H2O | interaction via HslV intact active site | Escherichia coli | ? | - |
? | |
additional information | analysis of interaction of free and inhibited HslV with HslU showing moderate affinity, scheme of substrate-induced HslUV assemblage, overview | Escherichia coli | ? | - |
? | |
N-carbobenzyloxy-Gly-Gly-Leu-7-amido-4-methylcoumarin + H2O | - |
Escherichia coli | N-carbobenzyloxy-Gly-Gly-Leu + 7-amino-4-methylcoumarin | - |
? | |
SulA-maltose binding protein-fusion protein + H2O | recombinant substrate, formation of a ternary complex of HslV-HslU-substrate during reaction, molecular interaction study, interaction via HslU, not HslV | Escherichia coli | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
HslU chaperone | - |
Escherichia coli |
HslUV complex | - |
Escherichia coli |
HslV peptidase | - |
Escherichia coli |
HslV protease | - |
Escherichia coli |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Escherichia coli |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | - |
assay at | Escherichia coli |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ATP | dependent on | Escherichia coli |