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Literature summary for 3.4.21.53 extracted from

  • Bissonnette, S.A.; Rivera-Rivera, I.; Sauer, R.T.; Baker, T.A.
    The IbpA and IbpB small heat-shock proteins are substrates of the AAA+ Lon protease (2010), Mol. Microbiol., 75, 1539-1549.
    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
0.016
-
 IbpB pH 8.0, 37°C Escherichia coli
0.016
-
 IbpB substrate lacking both C- and N-terminal tail, pH 8.0, 37°C Escherichia coli
0.017
-
 IbpA substrate lacking both C- and N-terminal tail, pH 8.0, 37°C Escherichia coli
0.018
-
 IbpA pH 8.0, 37°C Escherichia coli
0.026
-
 human alphaB-crystallin substrate lacking both C- and N-terminal tail, pH 8.0, 37°C Escherichia coli
0.035
-
 human alphaA-crystallin substrate lacking both C- and N-terminal tail, pH 8.0, 37°C Escherichia coli
0.05
-
 human alphaA-crystallin pH 8.0, 37°C Escherichia coli
0.058
-
 human alphaB-crystallin 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 alphaA-crystallin + H2O Lon recognizes conserved determinants in the folded alpha-crystallin domain itself Escherichia coli ?
-
 ?
human alphaB-crystallin + H2O Lon recognizes conserved determinants in the folded alpha-crystallin domain itself Escherichia coli ?
-
 ?
IbpA + H2O i.e. Escherichia coli small heat shock protein A. Lon degrades purified IbpA substantially more slowly than purified IbpB, which is a consequence of differences in maximal Lon degradation rates and not in substrate affinity. IbpB stimulates Lon degradation of IbpA both in vitro and in vivo. The variable N- and C-terminal tails of the Ibps contain critical determinants that control the maximal rate of Lon degradation Escherichia coli ?
-
 ?
IbpB + H2O i.e. Escherichia coli small heat shock protein B. Lon degrades purified IbpA substantially more slowly than purified IbpB, which is a consequence of differences in maximal Lon degradation rates and not in substrate affinity.The variable N- and C-terminal tails of the Ibps contain critical determinants that control the maximal rate of Lon degradation Escherichia coli ?
-
 ?