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Literature summary for 3.4.21.53 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
Search for more literature for 3.4.21.53

Cloned(Commentary)

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

General Stability

General Stability Organism
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
hLon ist rapidly digested by trypsin, ADP binding does not protect Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
ADP non-competitive inhibition, ELon binds to ADP and undergoes at least one structural change that exposes a tryptic digestion site Escherichia coli
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]

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

Localization

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

Organism

Organism UniProt Comment Textmining
Escherichia coli P0A9M0
-
-
Homo sapiens P36776
-
-

Purification (Commentary)

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
FRETN 89-98 + H2O
-
 Homo sapiens ?
-
 ?
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 ?
-
 ?
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

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

Synonyms

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

Temperature Optimum [°C]

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

Turnover Number [1/s]

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

pH Optimum

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

Ki Value [mM]

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

General Information

General Information Comment Organism
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
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
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]

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