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Literature summary for 3.4.21.53 extracted from

  • Redelberger, D.; Genest, O.; Arabet, D.; Mejean, V.; Ilbert, M.; Iobbi-Nivol, C.
    Quality control of a molybdoenzyme by the Lon protease (2013), FEBS Lett., 587, 3935-3942.
    View publication on PubMed
Search for more literature for 3.4.21.53

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression of His6-tagged enzyme Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
TorD impairs the enzyme's TorA degradation activity by binding to apoTorA Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
apoTorA + H2O Escherichia coli a molybdoenzyme; immature TorA (apoTorA) is degraded in vivo and in vitro by the Lon protease. Enzyme Lon interacts with apoTorA but not with holoTorA. Enzyme Lon and TorD, the specific chaperone of TorA, compete for apoTorA binding, but TorD binding protects apoTorA against degradation ?
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His6-tagged enzyme by affinity chromatography Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
apoTorA + H2O a molybdoenzyme; immature TorA (apoTorA) is degraded in vivo and in vitro by the Lon protease. Enzyme Lon interacts with apoTorA but not with holoTorA. Enzyme Lon and TorD, the specific chaperone of TorA, compete for apoTorA binding, but TorD binding protects apoTorA against degradation Escherichia coli ?
-
 ?
apoTorA + H2O a molybdoenzyme, immature TorA (apoTorA) is degraded in vivo and in vitro by the Lon protease. Enzyme Lon interacts with apoTorA but not with holoTorA. Enzyme Lon and TorD, the specific chaperone of TorA, compete for apoTorA binding, but TorD binding protects apoTorA against degradation Escherichia coli ?
-
 ?

Synonyms

Synonyms Comment Organism
lon protease
-
 Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
 assay at Escherichia coli

General Information

General Information Comment Organism
physiological function protease Lon eliminates an immature or misfolded molybdoenzyme probably by targeting its inactive catalytic site, it is involved in the apoTorA degradation process Escherichia coli