Activating Compound | Comment | Organism | Structure |
---|---|---|---|
adenosine-5'-(beta,gamma-imido)triphosphate | slight activation | Escherichia coli |
Protein Variants | Comment | Organism |
---|---|---|
R164A | site-directed mutagenesis, the ATPase activity of the mutant is markedly reduced compared to the wild-type enzyme, thhe mutant retains the ability to hydrolyze PepTBE in the absence of effectors | Escherichia coli |
R542A | site-directed mutagenesis, the mutant completely loses its ability to hydrolyze ATP, the mutant retains the ability to hydrolyze PepTBE in the absence of effectors | Escherichia coli |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
ADP | - |
Escherichia coli | |
ATP | - |
Escherichia coli |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | activates, presence of free Mg2+ ions inhibits the ATPase activity of the enzyme, the effect is eliminated in the presence of the protein substrate | Escherichia coli |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | Escherichia coli | homooligomeric ATP-dependent LonA proteases are bifunctional enzymes | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
beta-casein + H2O | - |
Escherichia coli | ? | - |
? | |
Melittin + H2O | - |
Escherichia coli | ? | - |
? | |
additional information | homooligomeric ATP-dependent LonA proteases are bifunctional enzymes | Escherichia coli | ? | - |
? | |
additional information | native enzyme hydrolyzes ATP in the absence of a protein substrate | Escherichia coli | ? | - |
? | |
Suc-Phe-Leu-Phe-SBzl + H2O | a N-substituted tripeptide substrate | Escherichia coli | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
homooligomer | the subunits are formed by five successively connected domains, i.e., N-terminal domain, alpha-helical domain, nucleotide-binding domain, second alpha-helical domain, and proteolytic domain, domain organization, overview | Escherichia coli |
Synonyms | Comment | Organism |
---|---|---|
ATP-dependent lon protease | - |
Escherichia coli |
EcLon | - |
Escherichia coli |
lon protease | - |
Escherichia coli |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Escherichia coli |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8.1 | - |
assay at | Escherichia coli |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ATP | dependent on | Escherichia coli |
General Information | Comment | Organism |
---|---|---|
evolution | homooligomeric ATP-dependent LonA proteases are bifunctional enzymes belonging to the superfamily of AAA+ proteins | Escherichia coli |
additional information | the second alpha-helical domain plays a crucial role in ATP hydrolysis and enzyme binding to the target protein, while the first alpha-helical domain is not important for the manifestation of the catalytic properties of the enzyme, but it affects the functioning of Lon ATPase and peptidase sites and is involved in maintaining enzyme stability, participation of the first alpha-helical domain in the formation of three-dimensional structures of LonA proteases and/or their complexes with DNA | Escherichia coli |
physiological function | the ATP-dependent Lon protease is a key component of the quality control system, which ensures the integrity and functionality of cellular proteins | Escherichia coli |