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Literature summary extracted from
- Functional mechanics of the ATP-dependent Lon protease- lessons from endogenous protein and synthetic peptide substrates (2008), Biochim. Biophys. Acta, 1784, 727-735.
Activating Compound
| EC Number | Activating Compound | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.4.21.53 | additional information | oligomerization is stimulated by unfolded protein | Mycolicibacterium smegmatis | |
| 3.4.21.53 | additional information | protein substrate stimulates DNA binding | Homo sapiens | |
| 3.4.21.53 | Polyphosphate | stimulates lon-mediated proteolysis of free ribosomal proteins and thereby down-regulates translation | Escherichia coli |  |
Application
| EC Number | Application | Comment | Organism |
|---|---|---|---|
| 3.4.21.53 | additional information | functions in protein quality control | Escherichia coli |
| 3.4.21.53 | additional information | induction of lon contributes to the adaptive resistance of the organism towards antibiotic treatment | Pseudomonas aeruginosa |
| 3.4.21.53 | additional information | stress response network between the endoplasmic reticulum, nucleus and mitochondrion up-regulates the expression, thereby providing a cytoprotective function during endoplasmic reticulum stress and hypoxia | Homo sapiens |
| 3.4.21.53 | additional information | stress response network between the endoplasmic reticulum, nucleus and mitochondrion up-regulates the expression, thereby providing a cytoprotective function during endoplasmic reticulum stress and hypoxia | Rattus norvegicus |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 3.4.21.53 | E614K | mixed oligomeric complexes composed of wild-type lon and the inactive lon E614K mutant, results in an enzymatically inactive protein | Escherichia coli |
| 3.4.21.53 | additional information | absence of lon, results in a lack of ATP-dependent proteolysis in the mitochondrial matrix, accumulation of electron dense aggregates and large mitochondrial DNA deletions. Mutant lacking both ATPase and protease activity also fails to suppress COX assembly defects | Saccharomyces cerevisiae |
| 3.4.21.53 | additional information | lon gene mutants, form long undivided filaments upon UV irradiation | Escherichia coli |
| 3.4.21.53 | additional information | lon-depleted cells show little if any mitochondrial DNA damage | Homo sapiens |
| 3.4.21.53 | S679W | proteolytically inactive mutant. ATPase activity is affected by a variety of mutations generated at the vicinity of the proteolytic site Ser 679. Mutation of the ATP-binding site abolishes both the ATPase and protease activities of lon | Escherichia coli |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.4.21.53 | anti-sense morpholino oligonucleotide | causes defects in mitochondrial membrane potential, respiration and morphology, as well as apoptotic cell death | Homo sapiens | |
| 3.4.21.53 | ATP | ATP-binding inhibits DNA binding | Homo sapiens | |
| 3.4.21.53 | bacteriophage T4 PinA protein | specifically inhibits Escherichia coli Lon | Escherichia coli | |
| 3.4.21.53 | MG262 | i.e. Cb2-Leu-Leu-Leu-bornic acid | Salmonella enterica subsp. enterica serovar Typhimurium | |
| 3.4.21.53 | additional information | expression of an inducible short hairpin RNA leading to lon depletion in a colon adenocarcinoma cell line for 14 days does not lead to cell death. Even after RNAi knockdown for 3 weeks, these cells continue to survive, although they no longer proliferate | Homo sapiens | |
| 3.4.21.53 | Polyphosphate | competitively blocks DNA binding by lon in vitro and in vivo | Escherichia coli | |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 3.4.21.53 | cytosol | - |
Escherichia coli | 5829 | - |
| 3.4.21.53 | mitochondrion | - |
Homo sapiens | 5739 | - |
| 3.4.21.53 | mitochondrion | - |
Rattus norvegicus | 5739 | - |
| 3.4.21.53 | mitochondrion | - |
Saccharomyces cerevisiae | 5739 | - |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.4.21.53 | Mg2+ | oligomerization is dependent on Mg2+ | Escherichia coli | |
| 3.4.21.53 | Mg2+ | oligomerization is dependent on Mg2+ | Mycolicibacterium smegmatis | |
| 3.4.21.53 | additional information | maintenance of the holoenzyme does not require the addition of Mg2+ | Saccharomyces cerevisiae |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.4.21.53 | Brucella abortus | - |
- |
- |
| 3.4.21.53 | Caulobacter vibrioides | - |
- |
- |
| 3.4.21.53 | Escherichia coli | - |
- |
- |
| 3.4.21.53 | Homo sapiens | - |
- |
- |
| 3.4.21.53 | Mycolicibacterium smegmatis | - |
- |
- |
| 3.4.21.53 | Pseudomonas aeruginosa | - |
- |
- |
| 3.4.21.53 | Rattus norvegicus | - |
- |
- |
| 3.4.21.53 | Saccharomyces cerevisiae | - |
- |
- |
| 3.4.21.53 | Salmonella enterica subsp. enterica serovar Typhimurium | - |
- |
- |
| 3.4.21.53 | Thermoplasma acidophilum | - |
- |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 3.4.21.53 | - |
Escherichia coli |
| 3.4.21.53 | - |
Saccharomyces cerevisiae |
| 3.4.21.53 | - |
Mycolicibacterium smegmatis |
Source Tissue
| EC Number | Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|---|
| 3.4.21.53 | colonic adenocarcinoma cell line | - |
Homo sapiens | - |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.4.21.53 | bacteriophage lambda N protein + H2O | - |
Escherichia coli | ? | - |
? | |
| 3.4.21.53 | casein + H2O | - |
Escherichia coli | ? | - |
? | |
| 3.4.21.53 | CcdA + H2O | - |
Escherichia coli | ? | - |
? | |
| 3.4.21.53 | Cox4-1 + H2O | - |
Homo sapiens | ? | - |
? | |
| 3.4.21.53 | DNA methyltransferase + H2O | selectively degrades cell-cycle-regulated DNA methyltransferase thereby regulating methylation of chromosomal DNA and cellular differentiation | Caulobacter vibrioides | ? | - |
? | |
| 3.4.21.53 | HilA + H2O | mediates proteolysis of the central transcription regulatory factor HilA, which controls the correct timing for the expression of virulence genes necessary for host invasion | Salmonella enterica subsp. enterica serovar Typhimurium | ? | - |
? | |
| 3.4.21.53 | HilA + H2O | mediates proteolysis of the central transcription regulatory factor HilA, which controls the correct timing for the expression of virulence genes necessary for host invasion | Brucella abortus | ? | - |
? | |
| 3.4.21.53 | mitochondrial processing peptidase alpha subunit + H2O | is degraded only when it is folded, trypsin-resistant and competent for assembly into an active enzyme | Homo sapiens | ? | - |
? | |
| 3.4.21.53 | additional information | endogenous substrates, which are misfolded or unassembled subunits of electron transport chain complexes, ribosomal proteins and metabolic enzymes | Saccharomyces cerevisiae | ? | - |
? | |
| 3.4.21.53 | Rcs + H2O | - |
Escherichia coli | ? | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 3.4.21.53 | heptamer | cryoelectron microscopy and analytic ultracentrifugation | Saccharomyces cerevisiae |
| 3.4.21.53 | hexamer | analytical ultracentrifugation | Mycolicibacterium smegmatis |
| 3.4.21.53 | hexamer | electron microscopy | Escherichia coli |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.4.21.53 | ATP-dependent lon protease | - |
Salmonella enterica subsp. enterica serovar Typhimurium |
| 3.4.21.53 | ATP-dependent lon protease | - |
Escherichia coli |
| 3.4.21.53 | ATP-dependent lon protease | - |
Homo sapiens |
| 3.4.21.53 | ATP-dependent lon protease | - |
Rattus norvegicus |
| 3.4.21.53 | ATP-dependent lon protease | - |
Saccharomyces cerevisiae |
| 3.4.21.53 | ATP-dependent lon protease | - |
Mycolicibacterium smegmatis |
| 3.4.21.53 | ATP-dependent lon protease | - |
Pseudomonas aeruginosa |
| 3.4.21.53 | ATP-dependent lon protease | - |
Thermoplasma acidophilum |
| 3.4.21.53 | ATP-dependent lon protease | - |
Brucella abortus |
| 3.4.21.53 | ATP-dependent lon protease | - |
Caulobacter vibrioides |
| 3.4.21.53 | lon | - |
Salmonella enterica subsp. enterica serovar Typhimurium |
| 3.4.21.53 | lon | - |
Escherichia coli |
| 3.4.21.53 | lon | - |
Homo sapiens |
| 3.4.21.53 | lon | - |
Rattus norvegicus |
| 3.4.21.53 | lon | - |
Saccharomyces cerevisiae |
| 3.4.21.53 | lon | - |
Mycolicibacterium smegmatis |
| 3.4.21.53 | lon | - |
Pseudomonas aeruginosa |
| 3.4.21.53 | lon | - |
Thermoplasma acidophilum |
| 3.4.21.53 | lon | - |
Brucella abortus |
| 3.4.21.53 | lon | - |
Caulobacter vibrioides |
| 3.4.21.53 | lon protease | - |
Salmonella enterica subsp. enterica serovar Typhimurium |
| 3.4.21.53 | lon protease | - |
Escherichia coli |
| 3.4.21.53 | lon protease | - |
Homo sapiens |
| 3.4.21.53 | lon protease | - |
Rattus norvegicus |
| 3.4.21.53 | lon protease | - |
Saccharomyces cerevisiae |
| 3.4.21.53 | lon protease | - |
Mycolicibacterium smegmatis |
| 3.4.21.53 | lon protease | - |
Pseudomonas aeruginosa |
| 3.4.21.53 | lon protease | - |
Thermoplasma acidophilum |
| 3.4.21.53 | lon protease | - |
Brucella abortus |
| 3.4.21.53 | lon protease | - |
Caulobacter vibrioides |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.4.21.53 | additional information | maintenance of the holoenzyme does not require the addition of ATP. ATP binding induces conformational changes in the holoenzyme | Saccharomyces cerevisiae | |
| 3.4.21.53 | additional information | oligomerization is independent of ATP | Escherichia coli | |
| 3.4.21.53 | additional information | oligomerization is independent of ATP | Mycolicibacterium smegmatis |
Ki Value [mM]
| EC Number | Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.4.21.53 | 0.0000066 | - |
MG262 | - |
Salmonella enterica subsp. enterica serovar Typhimurium | |
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