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Literature summary extracted from

  • Fishovitz, J.; Sha, Z.; Chilakala, S.; Cheng, I.; Xu, Y.; Lee, I.
    Utilization of mechanistic enzymology to evaluate the significance of ADP binding to human Lon protease (2017), Front. Mol. Biosci., 4, 47 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.4.21.53 gene lon Escherichia coli
3.4.21.53 gene LONP1, recombinant expression of the enzyme in Escherichia coli strain Rosetta (DE3) Homo sapiens

General Stability

EC Number General Stability Organism
3.4.21.53 ELon ist quite stable against digestion by trypsin, ADP binding does not protect. ELon binds to ADP and undergoes at least one structural change that exposes a tryptic digestion site Escherichia coli
3.4.21.53 hLon ist rapidly digested by trypsin, ADP binding does not protect Homo sapiens

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.21.53 ADP non-competitive inhibition, ELon binds to ADP and undergoes at least one structural change that exposes a tryptic digestion site Escherichia coli
3.4.21.53 ADP non-competitive inhibition dependent on substrate concentration, steady-state ADP inhibition study, overview. hLon binds to ADP and undergoes at least one structural change that exposes a tryptic digestion site Homo sapiens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.4.21.53 1.027
-
FRETN 89-98 pH 8.0, 37°C, recombinant enzyme Homo sapiens

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.4.21.53 cytosol
-
Escherichia coli 5829
-
3.4.21.53 mitochondrion
-
Homo sapiens 5739
-

Organism

EC Number Organism UniProt Comment Textmining
3.4.21.53 Escherichia coli P0A9M0
-
-
3.4.21.53 Homo sapiens P36776
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.4.21.53 recombinant enzyme from Escherichia coli strain Rosetta (DE3) by ultrafiltration and gel filtration Homo sapiens

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.21.53 FRETN 89-98 + H2O
-
Homo sapiens ?
-
?
3.4.21.53 additional information Lon protease has three activities: intrinsic ATPase, substrate-stimulated ATPase, and ATP-dependent proteolysis. Lon preferentially degrades damaged or misfolded proteins at its proteolytic site while the ATP is bound and hydrolyzed into ADP and phosphate at its ATPase site Homo sapiens ?
-
?
3.4.21.53 additional information Lon protease has three activities: intrinsic ATPase, substrate-stimulated ATPase, and ATP-dependent proteolysis. Lon preferentially degrades damaged or misfolded proteins at its proteolytic site while the ATP is bound and hydrolyzed into ADP and phosphate at its ATPase site Escherichia coli ?
-
?

Subunits

EC Number Subunits Comment Organism
3.4.21.53 ? x * 83000, recombinant enzyme, SDS-PAGE Escherichia coli

Synonyms

EC Number Synonyms Comment Organism
3.4.21.53 ATP-dependent protease La
-
Escherichia coli
3.4.21.53 ELon
-
Escherichia coli
3.4.21.53 hLon
-
Homo sapiens
3.4.21.53 lon
-
Homo sapiens
3.4.21.53 lon
-
Escherichia coli
3.4.21.53 lon protease
-
Homo sapiens
3.4.21.53 lon protease
-
Escherichia coli
3.4.21.53 LONP1
-
Homo sapiens
3.4.21.53 mitochondrial ATP-dependent protease La
-
Homo sapiens
3.4.21.53 Protease La
-
Homo sapiens
3.4.21.53 Protease La
-
Escherichia coli

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.4.21.53 37
-
assay at Escherichia coli
3.4.21.53 37
-
assay at Homo sapiens

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.4.21.53 6.63
-
FRETN 89-98 pH 8.0, 37°C, recombinant enzyme Homo sapiens

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.4.21.53 8
-
assay at Homo sapiens
3.4.21.53 8
-
assay at Escherichia coli

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
3.4.21.53 additional information
-
additional information steady-state kinetics, ADP inhibition study Homo sapiens
3.4.21.53 1.79
-
ADP pH 8.0, 37°C, recombinant enzyme Homo sapiens

General Information

EC Number General Information Comment Organism
3.4.21.53 evolution human enzyme hLon and Escherichia coli enzyme ELon bind to ADP and undergo at least one structural change that exposes the same tryptic digestion site, suggesting the presence of at least one conserved structural change in the two enzyme homologues upon binding to ADP Homo sapiens
3.4.21.53 evolution human enzyme hLon and Escherichia coli enzyme ELon bind to ADP and undergo at least one structural change that exposes the same tryptic digestion site, suggesting the presence of at least one conserved structural change in the two enzyme homologues upon binding to ADP Escherichia coli
3.4.21.53 physiological function in eukaryotes, Lon 1 is localized in the mitochondria and helps maintain proper cellular function. In humans, Lon is critical for maintaining the structure and integrity of mitochondria and has been found to selectively degrade accumulating proteins damaged by oxidative stress over their native counterparts Homo sapiens

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
3.4.21.53 6.46
-
FRETN 89-98 pH 8.0, 37°C, recombinant enzyme Homo sapiens