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Literature summary extracted from
- Characterization of the HslU chaperone affinity for HslV protease. [Erratum to document cited in CA143:073777] (2005), Protein Sci., 14, 2484.
No PubMed abstract available
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.4.25.2 | N-acetyl-Leu-Leu-norleucinal | i.e. calpain inhibitor-I, inhibits HslV | Escherichia coli |  |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.4.25.2 | additional information | - |
additional information | kinetics, analysis of interaction of free and inhibited HslV with HslU | Escherichia coli |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.4.25.2 | Mg2+ | - |
Escherichia coli | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.4.25.2 | Escherichia coli | - |
- |
- |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.4.25.2 | alpha-casein + H2O | interaction via HslV intact active site | Escherichia coli | ? | - |
? | |
| 3.4.25.2 | additional information | analysis of interaction of free and inhibited HslV with HslU showing moderate affinity, scheme of substrate-induced HslUV assemblage, overview | Escherichia coli | ? | - |
? | |
| 3.4.25.2 | N-carbobenzyloxy-Gly-Gly-Leu-7-amido-4-methylcoumarin + H2O | - |
Escherichia coli | N-carbobenzyloxy-Gly-Gly-Leu + 7-amino-4-methylcoumarin | - |
? | |
| 3.4.25.2 | 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
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.4.25.2 | HslU chaperone | - |
Escherichia coli |
| 3.4.25.2 | HslUV complex | - |
Escherichia coli |
| 3.4.25.2 | HslV peptidase | - |
Escherichia coli |
| 3.4.25.2 | HslV protease | - |
Escherichia coli |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.4.25.2 | 37 | - |
assay at | Escherichia coli |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.4.25.2 | 7.5 | - |
assay at | Escherichia coli |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.4.25.2 | ATP | dependent on | Escherichia coli | |
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