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Literature summary extracted from
- Recent developments in the mechanistic enzymology of the ATP-dependent Lon protease from Escherichia coli: highlights from kinetic studies (2006), Mol. Biosyst., 2, 477-483.
Activating Compound
| EC Number | Activating Compound | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.4.21.53 | additional information | degradation of proteins stimulates ATPase activity of lon | Escherichia coli | |
| 3.4.21.53 | Polyphosphate | its binding within the ATPase domain of lon promotes the specific association and degradation of free ribosomal proteins | Escherichia coli |  |
Application
| EC Number | Application | Comment | Organism |
|---|---|---|---|
| 3.4.21.53 | medicine | lon mediates proteolysis for the expression of virulence genes that promote mammalian cell infection | Salmonella enterica subsp. enterica serovar Typhimurium |
| 3.4.21.53 | medicine | lon mediates proteolysis for the expression of virulence genes that promote mammalian cell infection | Brucella abortus |
| 3.4.21.53 | additional information | plays vital roles in maintaining cellular functions by selectively eliminating misfolded, damaged and certain short-lived regulatory proteins. lon is essential for cellular homeostasis, mediating protein quality control and metabolic regulation | Escherichia coli |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.4.21.53 | ADP | inhibits proteolytic activity of lon | Escherichia coli | |
| 3.4.21.53 | MG 262 | is a potent peptide-based inhibitor | Salmonella enterica subsp. enterica serovar Typhimurium | |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 3.4.21.53 | mitochondrion | - |
Homo sapiens | 5739 | - |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.4.21.53 | Brucella abortus | - |
- |
- |
| 3.4.21.53 | Escherichia coli | - |
- |
- |
| 3.4.21.53 | Homo sapiens | - |
- |
- |
| 3.4.21.53 | Saccharomyces cerevisiae | - |
- |
- |
| 3.4.21.53 | Salmonella enterica subsp. enterica serovar Typhimurium | - |
- |
- |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.4.21.53 | DNA | mitochondrial lon binds preferentially to single-stranded DNA in a sequence-dependent manner | Homo sapiens | ? | - |
? | |
| 3.4.21.53 | mitochondrial processing peptidase alpha subunit + H2O | human lon initiates substrate cleavage at surface exposed sites, lon degrades mitochondrial processing peptidase alpha subunit only when it is folded | Homo sapiens | ? | - |
? | |
| 3.4.21.53 | ribosomal S2 protein + H2O | major lon cleavages sites within the bacterial S2 ribosomal protein located at the interior of the molecule | Escherichia coli | ? | - |
? | |
| 3.4.21.53 | RNA | mitochondrial lon binds preferentially to single-stranded RNA in a sequence-dependent manner | Homo sapiens | ? | - |
? | |
| 3.4.21.53 | S1 peptide + H2O | decapeptide S1 containing the amino acid residues 89-98 of the bacteriophage lambdaN transcription anti-termination factor, and a fluorescence donor-acceptor pair | Escherichia coli | ? | - |
? | |
| 3.4.21.53 | steroidogenic acute regulatory protein + H2O | human lon initiates substrate cleavage at surface exposed sites | Homo sapiens | ? | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 3.4.21.53 | heptamer | cryoelectron microscopy | Homo sapiens |
| 3.4.21.53 | heptamer | cryoelectron microscopy | Saccharomyces cerevisiae |
| 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 | - |
Saccharomyces cerevisiae |
| 3.4.21.53 | ATP-dependent lon protease | - |
Brucella abortus |
| 3.4.21.53 | lon | - |
Homo sapiens |
| 3.4.21.53 | lon | - |
Saccharomyces cerevisiae |
| 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 | - |
Saccharomyces cerevisiae |
| 3.4.21.53 | lon protease | - |
Brucella abortus |
| 3.4.21.53 | Pim1p | - |
Saccharomyces cerevisiae |
| 3.4.21.53 | Protease La | - |
Salmonella enterica subsp. enterica serovar Typhimurium |
| 3.4.21.53 | Protease La | - |
Escherichia coli |
| 3.4.21.53 | Protease La | - |
Homo sapiens |
| 3.4.21.53 | Protease La | - |
Saccharomyces cerevisiae |
| 3.4.21.53 | Protease La | - |
Brucella abortus |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.4.21.53 | ATP | - |
Escherichia coli | |
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