EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.4.25.2 | Escherichia coli | - |
- |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.4.25.2 | benzyloxycarbonyl-GGL-7-amido-4-methylcoumarin + H2O | - |
Escherichia coli | benzyloxycarbonyl-GGL + 7-amino-4-methylcoumarin | - |
? | |
3.4.25.2 | Insulin B-chain + H2O | HslVU degrades insulin B-chain even more rapidly in the presence of ATPgammaS than with ATP | Escherichia coli | ? | - |
? | |
3.4.25.2 | additional information | ATP-binding, but not its hydrolysis, is essential for assembly and proteolytic activity of HslVU | Escherichia coli | ? | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
3.4.25.2 | More | HslVU is an ATP-dependent protease consisting of two multimeric components: the HslU ATPase and the HslV peptidase | Escherichia coli |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
3.4.25.2 | adenosine 5'-(alpha,beta-methylene)triphosphate | HslVU degrades insulin B-chain more rapidly in the presence of ATPgammaS than with ATP | Escherichia coli | |
3.4.25.2 | ATP | ATP-binding, but not its hydrolysis, is essential for assembly and proteolytic activity of HslVU. The ability of ATP and its analogs in supporting the proteolytic activity is closely correlated with their ability in supporting the oligomerization of HslU and the formation of the HslVU complex | Escherichia coli | |
3.4.25.2 | ATPgammaS | HslVU degrades insulin B-chain more rapidly in the presence of ATPgammaS than with ATP | Escherichia coli | |
3.4.25.2 | beta,gamma-Imido-ATP | supports proteolytic activity to an extent less than 10% of that seen with ATP | Escherichia coli |