EC Number   |
Cofactor |
Reference |
|---|
   3.4.25.2 | 5'-adenylyl beta,gamma-imidotriphosphate |
can support peptide hydrolysis, but only after an initial time lag not seen with ATP. This delay decreases at higher temperatures and with higher HslV or HslU concentrations and is eliminated by preincubation of HslV and HslU together |
647876 |
| 3.4.25.2 | 5'-adenylyl beta,gamma-imidotriphosphate |
can support peptide hydrolysis, but only after an initial time lag not seen with ATP. This delay decreases at higher temperatures and with higher HslV or HslU concentrations and is eliminated by preincubation of HslV and HslU together. Supports hydrolysis of casein and other polypeptides only 20% as well as ATP. But in presence of K+, Cs+ or NH4+, activation of casein degradation is even better than that by ATP, although it is not hydrolyzed |
647876 |
| 3.4.25.2 | 5'-adenylyl beta,gamma-imidotriphosphate |
the enzyme degrades SulA and the fusion protein of SulA and maltose-binding protein in presence of ATP but not with ATPgammaS |
647882 |
| 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 |
647873 |
| 3.4.25.2 | ATP |
- |
666270, 733478, 734572 |
| 3.4.25.2 | ATP |
ATP activates hydrolysis of benzyloxycarbonyl-GGL-7-amido-4-methylcoumarin 150fold |
647880 |
| 3.4.25.2 | ATP |
ATP binding and hydrolysis are critical for protein degradation by HslUV, an AAA+ machine containing one or two HslU ATPases and the HslV peptidase. Asymmetric mechanism of ATP binding and hydrolysis. Molecular contacts between HslU and HslV vary dynamically throughout the ATPase cycle. Nucleotide binding controls HslUV assembly and activity. Binding of a single ATP allows HslU to bind HslV, whereas additional ATPs must bind HslU to support substrate recognition and to activate ATP hydrolysis, which powers substrate unfolding and translocation |
693651 |
| 3.4.25.2 | ATP |
ATP concentrations that activate hydrolysis of benzyloxycarbonyl-GGL-7-amido-4-methylcoumarin are 50-100fold lower than those necessary for degradation of proteins, e.g. casein. ATP binding to a high affinity site triggers the formation of an active state capable of peptide cleavage, although ATP hydrolysis facilitates this process |
647876 |
| 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 |
647873 |
| 3.4.25.2 | ATP |
dependent on |
666173, 666856, 712278, 712397, 713162, 719424, 720248, 734475 |
