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Literature summary for 3.4.21.53 extracted from

  • Spiridonova, V.; Kudzhaev, A.; Melnichuk, A.; Gainutdinov, A.; Andrianova, A.; Rotanova, T.
    Interaction of DNA aptamers with the ATP-dependent Lon protease from Escherichia coli (2015), Russ. J. Bioorg. Chem., 41, 626-630 .
    View publication on PubMed
Search for more literature for 3.4.21.53

Cloned(Commentary)

Cloned (Comment) Organism
gene lon, recombinant expression of His-tagged enzyme mutant in Escherichia coli Escherichia coli

Protein Variants

Protein Variants Comment Organism
S679A interaction analysis with thrombin-derived aptamers, overview Escherichia coli

Localization

Localization Comment Organism GeneOntology No. Textmining
cytosol
-
 Escherichia coli 5829
-

Organism

Organism UniProt Comment Textmining
Escherichia coli P0A9M0
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged enzyme mutant from Escherichia coli by nickel affinity chromatography and gel filtration Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information enzyme Ec-Lon interacts with DNA. Ec-Lon protease forms complexes with aptamers, obtained from thrombin, whose molecules comprise the duplex domains and G-quadruplex region. The aptamers have low affinities for the enzyme mutant S679A, the Lon protease does not show a strong ability to bind to any individual Gx02quadruplex (15TBA) or duplex aptamer (RE15T), but Lonx02 S679A forms complexes with twox02domain 31TBA, RE31 and ST43 aptamers Escherichia coli ?
-
 ?

Subunits

Subunits Comment Organism
homohexamer
-
 Escherichia coli
More the Ec-Lon subunit comprises N-terminal non-catalytic region, ATPase module and proteolytic domain (serine-lysine endopeptidase) Escherichia coli

Synonyms

Synonyms Comment Organism
ATP-dependent lon protease
-
 Escherichia coli
Ec-Lon
-
 Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 assay at Escherichia coli

General Information

General Information Comment Organism
metabolism ATP-dependent Lon protease of Escherichia coli (Ec-Lon) is a key enzyme of the quality control system of the cell proteome Escherichia coli
additional information the enzyme Ec-Lon is a bifunctional homohexameric enzyme, its subunit comprises an N-terminal noncatalytic region, two-domain ATPase module, and a proteolytic domain with serine-lysine endopeptidase activity Escherichia coli