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Literature summary for 3.4.21.53 extracted from
- Protein unfolding and degradation by the AAA+ Lon protease (2012), Protein Sci., 21, 268-278.
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.007 | - |
beta-galactosidase-93-titinI27 | pH not specified in the publication, 37°C | Escherichia coli | |
| 0.015 | - |
titinI27-beta-galactosidase-93 | pH not specified in the publication, 37°C | Escherichia coli | |
| 0.023 | - |
titinI27-beta-galactosidase-93-titinI27 | pH not specified in the publication, 37°C | Escherichia coli |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | Escherichia coli | repeated cycles of ATP binding and hydrolysis power conformational changes that pull the tag through the pore and eventually tug the native portion of the substrate against the AAA+ ring, creating an unfolding force. Depending on the native substrate and enzyme, successful unfolding can require anywhere from a few to many hundreds of cycles of ATP hydrolysis | ? | - |
? |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| beta-galactosidase-93-titinI27 + H2O | - |
Escherichia coli | ? | - |
? | |
| GFP-titinI27-sul20C + H2O | when degradation initiated at the N-terminus, the full-length substrate disappears about 10fold more rapidly than when degradation initiated at the C-terminus | Escherichia coli | ? | - |
? | |
| mDHFR protein + H2O | sul20C-tagged protein, degradation | Escherichia coli | ? | - |
? | |
| mDHFR protein + H2O | tittinI27-fusion and sul20C-tagged protein, to direct Lon degradation of a titinI27 domain, either the N or C terminus of this protein is fused to amino acids 3-93 of Escherichia coli beta-galactosidase, an unstructured sequence that contains the b20 degron, degradation | Escherichia coli | ? | - |
? | |
| additional information | repeated cycles of ATP binding and hydrolysis power conformational changes that pull the tag through the pore and eventually tug the native portion of the substrate against the AAA+ ring, creating an unfolding force. Depending on the native substrate and enzyme, successful unfolding can require anywhere from a few to many hundreds of cycles of ATP hydrolysis | Escherichia coli | ? | - |
? | |
| additional information | substrate specifiicty, overview. GFP-fusion proteins resist Lon degradation from the N-terminus. Partially degraded substrate fragments accumulate as proteolytic products, which is often observed during degradation in vitro of multi-domain substrates containing very stable interior domains | Escherichia coli | ? | - |
? | |
| titinI27-beta-galactosidase-93 + H2O | - |
Escherichia coli | ? | - |
? | |
| titinI27-beta-galactosidase-93-titinI27 + H2O | - |
Escherichia coli | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| AAA+ Lon protease | - |
Escherichia coli |
| AAA+ protease | - |
Escherichia coli |
| lon | - |
Escherichia coli |
| lon protease | - |
Escherichia coli |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
assay at, in vivo | Escherichia coli |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| ATP | dependent on | Escherichia coli | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | evolution has diversified rather than optimized the protein unfolding activities of different AAA+ proteases, Escherichia coli utilizes five different AAA+ proteases: Lon, ClpXP, ClpAP, HslUV, and FtsH | Escherichia coli |
| physiological function | AAA+ proteases employ a hexameric ring that harnesses the energy of ATP binding and hydrolysis to unfold native substrates and translocate the unfolded polypeptide into an interior compartment for degradation. Ability of theLon protease to unfold and degrade model protein substrates beginning at N-terminal, C-terminal, or internal degrons, unfolding with robust and processive unfolding/degradation of some substrates with very stable protein domains, including mDHFR and titin, overview | Escherichia coli |
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