EC Number | Cloned (Comment) | Organism |
---|---|---|
3.4.25.2 | HslU and HslV were coexpressed in BL21 (DE3) pLysS cells | Haemophilus influenzae |
3.4.25.2 | HslU and HslV were coexpressed in BL21 (DE3) pLysS cells | Escherichia coli |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.4.25.2 | Escherichia coli | - |
- |
- |
3.4.25.2 | Haemophilus influenzae | - |
- |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.4.25.2 | barnase-DHFR fusion proteins + H2O | - |
Haemophilus influenzae | ? | - |
? | |
3.4.25.2 | barnase-DHFR fusion proteins + H2O | - |
Escherichia coli | ? | - |
? | |
3.4.25.2 | additional information | degradation of proteins in an ATP-dependent and tag-specific manner. For degradation from the N-terminus, HslUV has the strongest unfolding ability of all the bacterial proteases (unfolding abilities of the 26S proteasome), whereas for degradation from the C-terminus, HslUV is one of the weaker unfoldases. HslUV unfolds proteins more effectively when degrading from the N- towards the C-terminus than in the opposite direction | Haemophilus influenzae | ? | - |
? | |
3.4.25.2 | additional information | degradation of proteins in an ATP-dependent and tag-specific manner. For degradation from the N-terminus, HslUV has the strongest unfolding ability of all the bacterial proteases (unfolding abilities of the 26S proteasome), whereas for degradation from the C-terminus, HslUV is one of the weaker unfoldases. HslUV unfolds proteins more effectively when degrading from the N- towards the C-terminus than in the opposite direction | Escherichia coli | ? | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.4.25.2 | ClpYQ | - |
Haemophilus influenzae |
3.4.25.2 | ClpYQ | - |
Escherichia coli |
3.4.25.2 | HslUV | - |
Haemophilus influenzae |
3.4.25.2 | HslUV | - |
Escherichia coli |