EC Number   |
Substrates |
Organism |
Products |
Reversibility |
|---|
   3.4.25.2 | alpha-casein + H2O |
- |
Escherichia coli |
? |
- |
? |
| 3.4.25.2 | alpha-casein + H2O |
degradation |
Escherichia coli |
? |
- |
? |
| 3.4.25.2 | alpha-casein + H2O |
interaction via HslV intact active site |
Escherichia coli |
? |
- |
? |
| 3.4.25.2 | alpha-casein + H2O |
the structural features of the GYVG motif increase degrading activity |
Escherichia coli |
? |
- |
? |
| 3.4.25.2 | Arc + H2O |
- |
Escherichia coli |
? |
- |
? |
| 3.4.25.2 | Arc + H2O |
degradation |
Escherichia coli |
? |
- |
? |
| 3.4.25.2 | Arc + H2O |
repressor protein, specific degradation, especially at heat shock temperatures, recognition of sequences near the N-terminus of Arc and strong binding requiring Mg2+ and ATP for degradation |
Escherichia coli |
? |
- |
? |
| 3.4.25.2 | Arc + H2O |
N-terminal residues of Arc are important for HslUV degradation |
Escherichia coli |
? |
- |
? |
| 3.4.25.2 | Arc mutant I137A + H2O |
monomeric mutant, degradation |
Escherichia coli |
? |
- |
? |
| 3.4.25.2 | Arc repressor + H2O |
interaction of Arc substrates with HslU variants bearing mutations in the GYVG pore loop or the I domain, overview. N-terminal residues of Arc initially interact with the GYVG loop in the axial pore of HslU, while other portions of Arc contact disordered I-domain loops, residues 175-209, that project into the substrate-binding funnel above the pore |
Escherichia coli |
? |
- |
? |
