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Literature summary for 3.4.21.53 extracted from

  • Andrianova, A.; Kudzhaev, A.; Serova, O.; Dergousova, N.; Rotanova, T.
    Role of alpha-helical domains in functioning of ATP-dependent Lon protease of Escherichia coli (2014), Russ. J. Bioorg. Chem., 40, 620-627.
No PubMed abstract available
Search for more literature for 3.4.21.53

Activating Compound

Activating Compound Comment Organism Structure
adenosine-5'-(beta,gamma-imido)triphosphate slight activation Escherichia coli

Protein Variants

Protein Variants Comment Organism
R164A site-directed mutagenesis, the ATPase activity of the mutant is markedly reduced compared to the wild-type enzyme, thhe mutant retains the ability to hydrolyze PepTBE in the absence of effectors Escherichia coli
R542A site-directed mutagenesis, the mutant completely loses its ability to hydrolyze ATP, the mutant retains the ability to hydrolyze PepTBE in the absence of effectors Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
ADP
-
 Escherichia coli
ATP
-
 Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ activates, presence of free Mg2+ ions inhibits the ATPase activity of the enzyme, the effect is eliminated in the presence of the protein substrate Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Escherichia coli homooligomeric ATP-dependent LonA proteases are bifunctional enzymes ?
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
beta-casein + H2O
-
 Escherichia coli ?
-
 ?
Melittin + H2O
-
 Escherichia coli ?
-
 ?
additional information homooligomeric ATP-dependent LonA proteases are bifunctional enzymes Escherichia coli ?
-
 ?
additional information native enzyme hydrolyzes ATP in the absence of a protein substrate Escherichia coli ?
-
 ?
Suc-Phe-Leu-Phe-SBzl + H2O a N-substituted tripeptide substrate Escherichia coli ?
-
 ?

Subunits

Subunits Comment Organism
homooligomer the subunits are formed by five successively connected domains, i.e., N-terminal domain, alpha-helical domain, nucleotide-binding domain, second alpha-helical domain, and proteolytic domain, domain organization, overview Escherichia coli

Synonyms

Synonyms Comment Organism
ATP-dependent lon protease
-
 Escherichia coli
EcLon
-
 Escherichia coli
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
8.1
-
 assay at Escherichia coli

Cofactor

Cofactor Comment Organism Structure
ATP dependent on Escherichia coli

General Information

General Information Comment Organism
evolution homooligomeric ATP-dependent LonA proteases are bifunctional enzymes belonging to the superfamily of AAA+ proteins Escherichia coli
additional information the second alpha-helical domain plays a crucial role in ATP hydrolysis and enzyme binding to the target protein, while the first alpha-helical domain is not important for the manifestation of the catalytic properties of the enzyme, but it affects the functioning of Lon ATPase and peptidase sites and is involved in maintaining enzyme stability, participation of the first alpha-helical domain in the formation of three-dimensional structures of LonA proteases and/or their complexes with DNA Escherichia coli
physiological function the ATP-dependent Lon protease is a key component of the quality control system, which ensures the integrity and functionality of cellular proteins Escherichia coli