KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.0046 | - |
F-QLRSLNGEWRFAWFPAPEAV-Q | 37°C | Escherichia coli | |
0.016 | - |
QLRSLNGEWRFAWFPAPEAV | 37°C | Escherichia coli | |
0.073 | - |
beta-galactosidase fragment 3-93 | 37°C | Escherichia coli | |
0.3 | - |
titin-I27CD | 37°C | Escherichia coli |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | Escherichia coli | protease Lon recognizes specific sequences rich in aromatic residues that are accessible in unfolded polypeptides but hidden in most native structures. Denatured polypeptides lacking such sequences are poor substrates. Lon also unfolds and degrades stably folded proteins with accessible recognition tags. Lon can recognize multiple signals in unfolded polypeptides synergistically, resulting in nanomolar binding and a mechanism for discriminating irreversibly damaged proteins from transiently unfolded elements of structure | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
beta-galactosidase fragment 3-93 + H2O | a 48-residue N-terminal variant and a 33-residue C-terminal variant of beta-galactosidase fragment are degraded very slowly. Lon rapidly degrades a variant containing the 68 N-terminal residues and a variant containing the C-terminal 43 residues of the 3-93 fragment. Residues 49-68, QLRSLNGEWRFAWFPAPEAV play an important role in regocnition by Lon | Escherichia coli | ? | - |
? | |
EYLFRHSDNELLHWM + H2O | degraded at rates within 50% of the F-QLRSLNGEWRFAWFPAPEAV-Q peptide | Escherichia coli | ? | - |
? | |
F-QLRSLNGEWRFAWFPAPEAV-Q + H2O | residues 4968 of betqa-galactosidase flanked by a fluorophore-quencher pair | Escherichia coli | F-QLRSLNG + EWRFAWFPAPEAV-Q | - |
? | |
FAKYWQAFRQYPRLQ + H2O | degraded considerably faster than the F-QLRSLNGEWRFAWFPAPEAV-Q peptide | Escherichia coli | ? | - |
? | |
FRQYPRLQGGFVWDW + H2O | degraded at rates within 30% of the F-QLRSLNGEWRFAWFPAPEAV-Q peptide | Escherichia coli | ? | - |
? | |
FVWDWVDQSLIKYDE + H2O | very slow degradation | Escherichia coli | ? | - |
? | |
HQWRGDFQFNISRYS + H2O | degraded at rates within 30% of the F-QLRSLNGEWRFAWFPAPEAV-Q peptide | Escherichia coli | ? | - |
? | |
HYPNHPLWYTLCDRY + H2O | degraded at rates within 50% of the F-QLRSLNGEWRFAWFPAPEAV-Q peptide | Escherichia coli | ? | - |
? | |
LLIRGVNRHEHHPLH + H2O | degraded at rates within 50% of the F-QLRSLNGEWRFAWFPAPEAV-Q peptide | Escherichia coli | ? | - |
? | |
LRAGENRLAVMVLRW + H2O | degraded at rates within 50% of the F-QLRSLNGEWRFAWFPAPEAV-Q peptide | Escherichia coli | ? | - |
? | |
LTEAKHQQQFFQFRL + H2O | degraded at rates within 50% of the F-QLRSLNGEWRFAWFPAPEAV-Q peptide | Escherichia coli | ? | - |
? | |
additional information | protease Lon recognizes specific sequences rich in aromatic residues that are accessible in unfolded polypeptides but hidden in most native structures. Denatured polypeptides lacking such sequences are poor substrates. Lon also unfolds and degrades stably folded proteins with accessible recognition tags. Lon can recognize multiple signals in unfolded polypeptides synergistically, resulting in nanomolar binding and a mechanism for discriminating irreversibly damaged proteins from transiently unfolded elements of structure | Escherichia coli | ? | - |
? | |
MWRMSGIFRDVSLLH + H2O | degraded at rates within 50% of the F-QLRSLNGEWRFAWFPAPEAV-Q peptide | Escherichia coli | ? | - |
? | |
QLRSLNGEWRFAWFPAPEAV + H2O | variant of the I27 domain of human titin containing aspartic acids in place of both wild-type cysteines and fused with residues 49-68 of beta-galactosidase fragment 3-93 | Escherichia coli | QLRSLNG + EWRFAWFPAPEAV | - |
? | |
RMVQRDRNHPSVIIW + H2O | degraded at rates within 50% of the F-QLRSLNGEWRFAWFPAPEAV-Q peptide | Escherichia coli | ? | - |
? | |
RWDLPLSDMYTPYVF + H2O | degraded at rates within 50% of the F-QLRSLNGEWRFAWFPAPEAV-Q peptide | Escherichia coli | ? | - |
? | |
RWLPAMSERVTRMVQ + H2O | degraded at rates within 50% of the F-QLRSLNGEWRFAWFPAPEAV-Q peptide | Escherichia coli | ? | - |
? | |
RWQFNRQSGFLSQMW + H2O | degraded considerably faster than the F-QLRSLNGEWRFAWFPAPEAV-Q peptide | Escherichia coli | ? | - |
? | |
titin-I27CD + H2O | variant of the I27 domain of human titin containing aspartic acids in place of both wild-type cysteines | Escherichia coli | ? | - |
? | |
YLEDQDMWRMSGIFR + H2O | degraded at rates within 50% of the F-QLRSLNGEWRFAWFPAPEAV-Q peptide | Escherichia coli | ? | - |
? | |
YWQAFRQYPRLQGGF + H2O | degraded considerably faster than the F-QLRSLNGEWRFAWFPAPEAV-Q peptide | Escherichia coli | ? | - |
? |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.84 | - |
beta-galactosidase fragment 3-93 | 37°C | Escherichia coli |