Activating Compound | Comment | Organism | Structure |
---|---|---|---|
ATP | hydrolysis of FITC casein is 10fold increase in presence of ATP | Thermoplasma acidophilum |
Protein Variants | Comment | Organism |
---|---|---|
D241A | 99% of wild-type peptidase activity | Thermoplasma acidophilum |
K63A | 113% of wild-type peptidase activity | Thermoplasma acidophilum |
additional information | Walker A and B motifs, and the sensor 1 and sensor 2 are essential for the ATPase activity, while sensor 2 and the arginine finger are involved in activation of the protease domain | Thermoplasma acidophilum |
N293A | 122% of wild-type peptidase activity | Thermoplasma acidophilum |
R305A | 2% of wild-type peptidase activity | Thermoplasma acidophilum |
R375A | 112% of wild-type peptidase activity | Thermoplasma acidophilum |
R382A | 6% of wild-type peptidase activity | Thermoplasma acidophilum |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
ADP | wild-type, up to 60% inhibition, mutant K63A, slight activation, mutants D241A, N293A, R375A, about 50% inhibition of peptidase activity. Complete inhibition of hydrolysis of FITC | Thermoplasma acidophilum | |
ATP | peptidase activity of enzyme is modulated by the ATP-state of the AAA+ domain. Absence of nucleotide results in basal activity, presence of ATP reduces the basal activity. Presence of ATP stimulates hydrolysis of FITC 10fold | Thermoplasma acidophilum |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
membrane | native enzyme and recombinant enzyme in Escherichia coli | Thermoplasma acidophilum | 16020 | - |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
72000 | - |
6 * 72000, SDS-PAGE | Thermoplasma acidophilum |
430000 | - |
gel filtration | Thermoplasma acidophilum |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Thermoplasma acidophilum | - |
- |
- |
Purification (Comment) | Organism |
---|---|
recombinant membrane enzyme in Escherichia coli | Thermoplasma acidophilum |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
additional information | - |
enzyme degrades substrates in a processive manner | Thermoplasma acidophilum |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
FITC casein + H2O | presence of ATP stimulates reaction 10fold | Thermoplasma acidophilum | ? | - |
? | |
N-succinyl-LLVY-7-amido-4-methylcoumarin + H2O | no cleavage of bond between Y and 7-amido-4-methylcoumarin | Thermoplasma acidophilum | N-succinyl-L-leucyl-L-leucine + Val-Tyr-7-amido-4-methylcoumarin + N-succinyl-L-leucine + Leu-Val-Tyr-7-amido-4-methylcoumarin | - |
? |
Subunits | Comment | Organism |
---|---|---|
hexamer | 6 * 72000, SDS-PAGE | Thermoplasma acidophilum |