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Literature summary for 3.4.21.53 extracted from

  • Sepuri, N.B.V.; Angireddy, R.; Srinivasan, S.; Guha, M.; Spear, J.; Lu, B.; Anandatheerthavarada, H.K.; Suzuki, C.K.; Avadhani, N.G.
    Mitochondrial LON protease-dependent degradation of cytochrome c oxidase subunits under hypoxia and myocardial ischemia (2017), Biochim. Biophys. Acta, 1858, 519-528 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.21.53

Cloned(Commentary)

Cloned (Comment) Organism
gene LONP1, recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3) Codon Plus (RIL) in inclusion bodies Mus musculus
gene LONP1, recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3) Codon Plus (RIL) in inclusion bodies Oryctolagus cuniculus

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion
-
 Mus musculus 5739
-
mitochondrion
-
 Oryctolagus cuniculus 5739
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
cytochrome c oxidase subunit + H2O Mus musculus
-
 ?
-
 ?
cytochrome c oxidase subunit + H2O Oryctolagus cuniculus
-
 ?
-
 ?

Organism

Organism UniProt Comment Textmining
Mus musculus Q8CGK3
-
-
Oryctolagus cuniculus G1TBZ8
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His6-tagged enzyme, solubilized from Escherichia coli strain BL21(DE3) Codon Plus (RIL) inclusion bodies, by nickel affinity chromatography Mus musculus
recombinant His6-tagged enzyme, solubilized from Escherichia coli strain BL21(DE3) Codon Plus (RIL) inclusion bodies, by nickel affinity chromatography Oryctolagus cuniculus

Renatured (Commentary)

Renatured (Comment) Organism
recombinangt His-tagged enzyme from inclusion bodies in Escherichia coli strain BL21(DE3) Codon Plus (RIL) by solubilization in in 50 mM Tris-HCl, pH 8.0, containing 8 M urea. The urea solubilized protein is refolded by dialyzing the protein for 3 h in each of 50 mM Tris-HCl pH 8.0, 1 mM 2-mercaptoethanol buffer containing 6 M, 4 M, 2 M, 1 M, and 100 mM urea, respectively with 0.075% deoxycholate. Finally, the storage buffer (20 mM Tris-HCl, pH 8.0, 1 mM 2-mercaptoethanol, 10% glycerol, 0.075% deoxycholate) without urea is used for dialysis Mus musculus
recombinangt His-tagged enzyme from inclusion bodies in Escherichia coli strain BL21(DE3) Codon Plus (RIL) by solubilization in in 50 mM Tris-HCl, pH 8.0, containing 8 M urea. The urea solubilized protein is refolded by dialyzing the protein for 3 h in each of 50 mM Tris-HCl pH 8.0, 1 mM 2-mercaptoethanol buffer containing 6 M, 4 M, 2 M, 1 M, and 100 mM urea, respectively with 0.075% deoxycholate. Finally, the storage buffer (20 mM Tris-HCl, pH 8.0, 1 mM 2-mercaptoethanol, 10% glycerol, 0.075% deoxycholate) without urea is used for dialysis Oryctolagus cuniculus

Source Tissue

Source Tissue Comment Organism Textmining
heart
-
 Oryctolagus cuniculus
-
macrophage
-
 Mus musculus
-
RAW-264.7 cell
-
 Mus musculus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
cytochrome c oxidase subunit + H2O
-
 Mus musculus ?
-
 ?
cytochrome c oxidase subunit + H2O
-
 Oryctolagus cuniculus ?
-
 ?
cytochrome c oxidase subunit IVi1 + H2O the phosphorylated IVi1 protein is degraded, while the phosphorylation-resistant S52A mutant protein is not degraded Mus musculus ?
-
 ?
cytochrome c oxidase subunit IVi1 + H2O the phosphorylated IVi1 protein is degraded, while the phosphorylation-resistant S52A mutant protein is not degraded Oryctolagus cuniculus ?
-
 ?
cytochrome c oxidase subunit Vb + H2O the phosphorylated Vb protein is degraded, while the phosphorylation-resistant S40A mutant protein is not degraded Mus musculus ?
-
 ?
cytochrome c oxidase subunit Vb + H2O the phosphorylated Vb protein is degraded, while the phosphorylation-resistant S40A mutant protein is not degraded Oryctolagus cuniculus ?
-
 ?
additional information three-dimensional modeling of cytochrome c oxidase (CcO)-Lon complex based on the X-ray crystal structures of bovine CcO complex and Escherichia coli Lon protein, interaction analysis, docking study Mus musculus ?
-
 ?
additional information three-dimensional modeling of cytochrome c oxidase (CcO)-Lon complex based on the X-ray crystal structures of bovine CcO complex and Escherichia coli Lon protein, interaction analysis, docking study Oryctolagus cuniculus ?
-
 ?

Synonyms

Synonyms Comment Organism
LONP1
-
 Mus musculus
LONRF1
-
 Oryctolagus cuniculus
mitochondrial Lon protease
-
 Mus musculus
mitochondrial Lon protease
-
 Oryctolagus cuniculus

General Information

General Information Comment Organism
physiological function mitochondrial LON protease-dependent degradation of cytochrome c oxidase (CcO) subunits under hypoxia and myocardial ischemia. Lon is involved in the preferential turnover of phosphorylated CcO subunits under hypoxic/ischemic stress. Role of Lon in the degradation of phosphorylated subunits of CcO complex and importance of phosphorylation sites S40 of Vb and T52 of IVi1 subunits in Lon mediated degradation Mus musculus
physiological function mitochondrial LON protease-dependent degradation of cytochrome c oxidase (CcO) subunits under hypoxia and myocardial ischemia. Lon is involved in the preferential turnover of phosphorylated CcO subunits under hypoxic/ischemic stress. Role of Lon in the degradation of phosphorylated subunits of CcO complex and importance of phosphorylation sites S40 of Vb and T52 of IVi1 subunits in Lon mediated degradation Oryctolagus cuniculus