Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.4.21.53 extracted from

  • Gur, E.; Sauer, R.T.
    Degrons in protein substrates program the speed and operating efficiency of the AAA+ Lon proteolytic machine (2009), Proc. Natl. Acad. Sci. USA, 106, 18503-18508.
    View publication on PubMedView publication on EuropePMC

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0022
-
human titin unfolded, bearing a sul20C peptide variant with an N-terminal PABA fluorophoreand a nitrotyrosine quencher at the penultimate C-terminal position followed by alanine at the C-terminus of the I27 domain, pH 8.0, 37°C Escherichia coli
0.024
-
human titin unfolded, bearing a 20-residue beta-galactosidase sequence at the C-terminus of the I27 domain, pH 8.0, 37°C Escherichia coli
0.04
-
human titin native, bearing C-terminal 20 residues of SulA sequence at the C-terminus of the I27 domain, pH 8.0, 37°C Escherichia coli
0.05
-
human titin native, bearing a 20-residue beta-galactosidase sequence at the C-terminus of the I27 domain, pH 8.0, 37°C Escherichia coli
0.053
-
human titin unfolded, bearing C-terminal 20 residues of SulA sequence at the C-terminus of the I27 domain, pH 8.0, 37°C Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
human titin + H2O
-
Escherichia coli ?
-
?
additional information enzyme recognizes degrons, i.e. degradation tags. Degron tags are also regulatory elements that determine protease activity levels. Different tags fused to the same protein change degradation speeds and energetic efficiencies by 10fold or more. Degron binding to multiple sites in the Lon hexamer differentially stabilizes specific enzyme conformations, including one with high protease and low ATPase activity, and results in positively cooperative degradation Escherichia coli ?
-
?