Cloned (Comment) | Organism |
---|---|
- |
Archaeoglobus fulgidus |
mutants cloned into vector pET24a(+), expressed in Escherichia coli Rosetta (DE3) pLysS | Archaeoglobus fulgidus |
Protein Variants | Comment | Organism |
---|---|---|
deltaTM(1)-lon-S509A | possesses neither proteolytic nor ATPase activity, is completely stable, can be considered as model of initial active delta TM(1)-lon forms | Archaeoglobus fulgidus |
deltaTM(2)-lon-S509A | possesses neither proteolytic nor ATPase activity, is completely stable, can be considered as model of initial active delta TM(2)-lon forms | Archaeoglobus fulgidus |
deltaTM1-lon | deletion of 100-186, leads to the removal of the predicted hydrophobic site of the transmembrane domain | Archaeoglobus fulgidus |
deltaTM2-lon | deletion of 119-222, leads to the removal of the predicted hydrophobic site of the transmembrane domain | Archaeoglobus fulgidus |
additional information | deletion of the transmembrane domain results in uncontrollable activation of the enzyme proteolytic site and in vivo autolysis yielding a stable and functionally inactive fragment consisting of both alpha-helical and proteolytic domains | Archaeoglobus fulgidus |
additional information | deletion of the transmembrane domain of LonB protease results in uncontrollable activation of the enzyme proteolytic site and in vivo autolysis yielding a stable and functionally inactive fragment consisting of both alpha-helical and proteolytic domains. The enzyme form with a transmembrane deletion and an additional site-directed mutagenesis at S509A (the catalytic Ser residue), is capable of recombination with the proteolytic-domain fragment. The mixed oligomers are proteolytically active, which indicates a crucial role of subunit interactions in the activation of the proteolytic site | Archaeoglobus fulgidus |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
36000 | - |
mutants deltaTM1-lon and deltaTM2-lon | Archaeoglobus fulgidus |
68200 | - |
x * 68200, the subunit consist of ATPase and proteolytic domains | Archaeoglobus fulgidus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Archaeoglobus fulgidus | - |
- |
- |
Archaeoglobus fulgidus | O29883 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + H2O | oligomeric organization of lon protease and ATP hydrolysis are necessary prerequisites of realization of the processive degradation of a protein substrate | Archaeoglobus fulgidus | phosphate + ADP | - |
? |
Subunits | Comment | Organism |
---|---|---|
oligomer | x * 68200, the subunit consist of ATPase and proteolytic domains | Archaeoglobus fulgidus |
Synonyms | Comment | Organism |
---|---|---|
AfLon | - |
Archaeoglobus fulgidus |
ATP-dependent lon protease | - |
Archaeoglobus fulgidus |
lonB protease | - |
Archaeoglobus fulgidus |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
70 | - |
- |
Archaeoglobus fulgidus |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
additional information | - |
thermophilic nature of lon protease is due to special features of enzyme activity regulation, structure of ATPase domain, and quaternary structure | Archaeoglobus fulgidus |
additional information | - |
the thermophilic nature of Lon protease is due to the special features of the enzyme activity regulation, the structure of ATPase domain, and the quaternary structure | Archaeoglobus fulgidus |