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Literature summary for 3.4.21.53 extracted from

  • Kudzhaev, A.; Andrianova, A.; Dubovtseva, E.; Serova, O.; Rotanova, T.
    Role of the inserted alpha-helical domain in E. coli ATP-dependent lon protease function (2017), Acta Naturae, 9, 75-81 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.21.53

Cloned(Commentary)

Cloned (Comment) Organism
gene lon, domain organization, overview Escherichia coli

Protein Variants

Protein Variants Comment Organism
additional information removal of the HI(CC) domain, deletion of the HI(CC) domain leads to a complete loss of the proteolytic activity towards beta-casein by the deletion form. The deletion form Lon-dHI(CC) is unstable and it undergoes autolysis both in the absence and presence of nucleotide effectors, the autolysis of Lon-dHI(CC) is most pronounced in the presence of Mg2+ ions Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
ADP
-
 Escherichia coli
Mg2+ excess of magnesium ions has an inhibitory effect on the hydrolysis of ATP Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required, activates, but excess of magnesium ions has an inhibitory effect on the hydrolysis of ATP Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P0A9M0
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
beta-casein + H2O
-
 Escherichia coli ?
-
 ?
additional information the enzyme is able to undergo autolysis and to bind DNA, analysis of formation of enzyme-DNA complexes Escherichia coli ?
-
 ?

Subunits

Subunits Comment Organism
More the inserted alpha-helical HI(CC) domain is necessary for the formation of the ATPase center of the Ec-Lon protease and its correct functioning Escherichia coli

Synonyms

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

Temperature Optimum [°C]

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

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.1
-
-
 Escherichia coli

Cofactor

Cofactor Comment Organism Structure
ATP required Escherichia coli

General Information

General Information Comment Organism
evolution the enzyme belongs to the protease fasmily S16 Escherichia coli
malfunction removal of the HI(CC) domain results in a dexadcrease in the activity of the peptidase center of the Ec-Lon protease and a loss of the regulatory effect of the ATPase center on the peptidase one, which is defined by the nature of the bound nucleotide in the intact enxadzyme. Deletion of the HI(CC) domain leads to a complete loss of the proteolytic activity towards beta-casein by the deletion form Escherichia coli
physiological function multidomain ATP-dependent Lon protease of Escherichia coli is one of the key enzymes of the quality control system of the cellular proteome. The HI(CC) domain of Ec-Lon protease is required for the formation of a functionally active enzyme structure and for the implementation of protein-protein interactions Escherichia coli