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Literature summary for 3.4.21.53 extracted from

  • Kereiche, S.; Kovacik, L.; Pevala, V.; Ambro, L.; Bellova, J.; Kutejova, E.; Raska, I.
    Three-dimensional reconstruction of the S885A mutant of human mitochondrial Lon protease (2014), Folia Biol. (Praha), 60 Suppl 1, 62-65.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression of His-tagged wild-type and mutant enzyme in Escherichia coli Homo sapiens

Protein Variants

Protein Variants Comment Organism
S885A site-directed mutagenesis, three-dimensional structure of the ADP-bound Lon S885A mutant obtained by electron microscopy as a result of preliminary negative staining studies Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion
-
Homo sapiens 5739
-

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ stabilizes the enzyme complex Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli by ultracentrifugation, nickel affinity chromatography and gel filtration Homo sapiens

Subunits

Subunits Comment Organism
hexamer or heptamer stabilized by Mg2+ and ADP bound to the ATPase region Homo sapiens

Synonyms

Synonyms Comment Organism
lon
-
Homo sapiens
lon protease
-
Homo sapiens
Lon protein
-
Homo sapiens

Cofactor

Cofactor Comment Organism Structure
ATP ADP bound to the ATPase region stabilizes the enzyme Homo sapiens

General Information

General Information Comment Organism
evolution the enzyme is a member of the ATPase superfamily Homo sapiens
malfunction altered expression levels of the enzyme are linked to some severe diseases such as epilepsy, myopathy, or lateral sclerosis Homo sapiens
physiological function the main function of the enzyme is the control of protein quality and the maintenance of proteostasis by degradation of misfolded and damaged proteins, which occur in response to numerous stress conditions. It also participates in the regulation of levels of transcription factors that control pathogenesis, development and stress response Homo sapiens