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Literature summary for 3.4.21.53 extracted from
- A membrane-bound archaeal Lon protease displays ATP-independent proteolytic activity towards unfolded proteins and ATP-dependent activity for folded proteins (2002), J. Bacteriol., 184, 3689-3698.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| LonTK cloned and expressed in Escherichia coli | Thermococcus kodakarensis |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| membrane | membrane-bound | Thermococcus kodakarensis | 16020 | - |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Ca2+ | - |
Thermococcus kodakarensis |  |
| Co2+ | supports the hydrolysis | Thermococcus kodakarensis | |
| Mg2+ | - |
Thermococcus kodakarensis | |
| Mn2+ | supports the hydrolysis | Thermococcus kodakarensis | |
| Ni2+ | serves as a cofactor better than Mg2+ and Ca2+ | Thermococcus kodakarensis | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 70000 | - |
SDS-PAGE | Thermococcus kodakarensis |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Thermococcus kodakarensis | Q8NKS6 | KOD1, previously called Pyrococcus kodakaraensis | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant enzyme | Thermococcus kodakarensis |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + H2O | - |
Thermococcus kodakarensis | phosphate + ADP | - |
? | |
| glutaryl-Ala-Ala-Phe-4-methoxy-beta-naphthylamide + H2O | - |
Thermococcus kodakarensis | ? | - |
? | |
| hemoglobin A + H2O | can degrade unfolded human hemoglobin A at 70°C either in presence or absence of ATP, at 37°C only in presence of ATP | Thermococcus kodakarensis | ? | - |
? | |
| additional information | belonging to AAA+ superfamily | Thermococcus kodakarensis | ? | - |
? | |
| ribulose-1,5-bisphosphate carboxylase/oxygenase + H2O | RubiscoTK | Thermococcus kodakarensis | ? | - |
? | |
| succinyl-Phe-Leu-Phe-4-methoxy-beta-naphthylamide + H2O | - |
Thermococcus kodakarensis | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| archaeal Lon protease | - |
Thermococcus kodakarensis |
| lon protease | - |
Thermococcus kodakarensis |
| lonTK | - |
Thermococcus kodakarensis |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 70 | - |
peptide cleavage activity | Thermococcus kodakarensis |
| 95 | - |
ATPase activity | Thermococcus kodakarensis |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 9 | - |
- |
Thermococcus kodakarensis |
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Release 2023.1 (January 2023)
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