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Literature summary for 3.4.21.53 extracted from
- A polyphosphate-lon protease complex in the adaptation of Escherichia coli to amino acid starvation (2006), Biosci. Biotechnol. Biochem., 70, 325-331.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| Polyphosphate | forms a complex with lon, which enables lon to degrade free ribosomal proteins. Polyphosphate with a shorter chain length is less potent in stimulating. Polyphosphate-binding site is within the ATPase domain fo lon between amino acids 320 and 437 | Escherichia coli |  |
Application
| Application | Comment | Organism |
|---|---|---|
| additional information | lon causes proteolysis of normal proteins in cells and is lethal to host cells. lon-polyphosphate complex is the missing link between protein degradation and the phenomen of stringent response. The complex between lon and polyphosphate is formed during the stringent response, whereon degrades at lest free ribosomal proteins, providing amino acids for synthesizing enzymes required for adaption to a nutrient-poor environment | Escherichia coli |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | lon clp ppk triple mutant, rate of protein turnover ist nearly identical to that of the lon clp double mutant. Deletion mutants of lon fused to the C-terminus of maltose-binding protein | Escherichia coli |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| Polyphosphate | slightly inhibits degradation of a maltose-binding protein-SulA fusion. At the ATP domain competes with DNA for binding to lon, completely inhibits the formation of a DNA-lon complex | Escherichia coli | |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| additional information | normally localized in nucleoids. Also present in polyphosphate granules of a phoU mutant, wich accumulates polyphosphate several 100fold higher than the wild-type | Escherichia coli | - |
- |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | Escherichia coli | the polyphosphate-lon complex does not degrade intact native ribosomes | ? | - |
? | |
| ribosomal S2 protein + H2O | Escherichia coli | - |
? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Escherichia coli |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| DNA | DNA-binding site of lon is the ATPase domain | Escherichia coli | ? | - |
? | |
| maltose-binding protein-SulA + H2O | - |
Escherichia coli | ? | - |
? | |
| additional information | the polyphosphate-lon complex does not degrade intact native ribosomes | Escherichia coli | ? | - |
? | |
| ribosomal S2 protein + H2O | - |
Escherichia coli | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| ATP-dependent lon protease | - |
Escherichia coli |
| lon | - |
Escherichia coli |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| ATP | - |
Escherichia coli | |
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