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Literature summary for 3.4.21.53 extracted from

  • Gur, E.; Sauer, R.T.
    Recognition of misfolded proteins by Lon, a AAA(+) protease (2008), Genes Dev., 22, 2267-2277.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.21.53

KM Value [mM]

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/ Products (Substrates)

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

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

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 49–68 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 [1/s]

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