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Literature summary for 3.4.21.53 extracted from

  • Lu, B.; Liu, T.; Crosby, J.A.; Thomas-Wohlever, J.; Lee, I.; Suzuki, C.K.
    The ATP-dependent Lon protease of Mus musculus is a DNA-binding protein that is functionally conserved between yeast and mammals (2003), Gene, 306, 45-55.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
Lon cDNA cloned and expressed in yeast strain PIM1, complementing a LON deletion, also overexpressed in COS-7 cells Mus musculus

Localization

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

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
100000
-
-
Homo sapiens
100000
-
immunoblotting Mus musculus

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
human
-
Mus musculus
-
mouse
-

Purification (Commentary)

Purification (Comment) Organism
-
Homo sapiens
recombinant enzyme Mus musculus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O
-
Mus musculus phosphate + ADP
-
?
ATP + H2O
-
Homo sapiens phosphate + ADP
-
?
additional information mediates the degradation of misfolded, unassembled or oxidatively damaged polypeptides, not only degrades protein substrates but also binds DNA, specifically binds to single stranded but not to double-stranded DNA oligonucleotides Mus musculus ?
-
?

Synonyms

Synonyms Comment Organism
lon protease
-
Mus musculus
lon protease
-
Homo sapiens