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Literature summary for 3.4.21.53 extracted from

  • Kudzhaev, A.; Dubovtseva, E.; Serova, O.; Andrianova, A.; Rotanova, T.
    Effect of the deletion of the (173-280) fragment of the inserted alpha-helical domain on the functional properties of ATP-dependent Lon protease from E. coli (2018), Russ. J. Bioorg. Chem., 44, 518-527 .
No PubMed abstract available
Search for more literature for 3.4.21.53

Protein Variants

Protein Variants Comment Organism
additional information construction of a recombinant form des-CC(G5)-Lon in which the deleted CC fragment, a deleted 108-unit coiled-coil fragment (residues M173-M280) is replaced by a pentaglycine peptide, the the ClpB chaperone of Thermus thermophilus. Analysis of enzymatic properties of des-CC(G5)-Lon-H6 (DELTArLon) mutant, overview. In the absence of nucleotide effectors as well as in the presence of free nucleotides or the ADP-Mg complex, casein is not hydrolyzed by rLon even if the duration of the experiment is increased many times. The deletion form DELTArLon is incapable of hydrolyzing beta-casein in the time interval in which the proteolytic activity of full-length rLon protease is tested Escherichia coli

Localization

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

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required, activates Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P0A9M0
-
-

Reaction

Reaction Comment Organism Reaction ID
hydrolysis of proteins in presence of ATP proteolysis mechanism, overview Escherichia coli
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
beta-casein + H2O
-
 Escherichia coli ?
-
 ?

Subunits

Subunits Comment Organism
More domain organization of Lon protease, overview Escherichia coli

Synonyms

Synonyms Comment Organism
ATP-dependent lon protease
-
 Escherichia coli
Ec-Lon
-
 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
8.5
-
 assay at Escherichia coli

Cofactor

Cofactor Comment Organism Structure
ATP dependent on Escherichia coli
additional information replacement of ATP by its non-hydrolyzable analogue (AMP-PNP) leads to a marked decrease in the substrate transformation rate and a change of the mechanism of casein hydrolysis for nonprocessive Escherichia coli

General Information

General Information Comment Organism
evolution the enzyme belongs to the protease family S16 and to the superfamily of AAA+ proteins Escherichia coli
malfunction the deletion form DELTArLon is incapable of hydrolyzing beta-casein in the time interval in which the proteolytic activity of full-length rLon protease is tested Escherichia coli
additional information the CC region is involved in the recognition of the nucleotide nature by the enzyme and the interaction of the enzyme with the protein substrate, effect of the coiled-coil (CC) region of the alpha-helical inserted domain of Escherichia coli Lon protease (Ec-Lon) on the functional activity of the enzyme, overview. The CC region is necessary for the formation and functioning of the ATPase and peptidase active centers, the occurrence of allosteric interactions between them, and for the implementation of proteolysis by a unique processive mechanism Escherichia coli
physiological function Lon protease is one of the main participants of the proteome quality control (PQC) system supporting normal cell homeostasis. The PQC system involves molecular chaperones participating in the remodeling and disaggregation of cellular proteins and ATP-dependent peptide hydrolases, which control the level of regulatory proteins through selective proteolysis and eliminate potentially hazardous, anomalous, defective, and redundant proteins from cells through their exhaustive degradation. All proteases of the PQC system are bifunctional enzymes whose proteolytic activity is coupled with the simultaneous ATP hydrolysis and is characterized by a processive mechanism of the hydrolysis of protein targets (without the release of high-molecular-weight intermediates) Escherichia coli