Literature summary for 3.4.21.53 extracted from

Lee, I.; Berdis, A.J.; Suzuki, C.K.
Recent developments in the mechanistic enzymology of the ATP-dependent Lon protease from Escherichia coli: highlights from kinetic studies (2006), Mol. Biosyst., 2, 477-483.

Search for more literature for 3.4.21.53

Activating Compound

Activating Compound	Comment	Organism	Structure
additional information	degradation of proteins stimulates ATPase activity of lon	Escherichia coli
Polyphosphate	its binding within the ATPase domain of lon promotes the specific association and degradation of free ribosomal proteins	Escherichia coli

Application

Application	Comment	Organism
medicine	lon mediates proteolysis for the expression of virulence genes that promote mammalian cell infection	Salmonella enterica subsp. enterica serovar Typhimurium
medicine	lon mediates proteolysis for the expression of virulence genes that promote mammalian cell infection	Brucella abortus
additional information	plays vital roles in maintaining cellular functions by selectively eliminating misfolded, damaged and certain short-lived regulatory proteins. lon is essential for cellular homeostasis, mediating protein quality control and metabolic regulation	Escherichia coli

Inhibitors

Inhibitors	Comment	Organism	Structure
ADP	inhibits proteolytic activity of lon	Escherichia coli
MG 262	is a potent peptide-based inhibitor	Salmonella enterica subsp. enterica serovar Typhimurium

Localization

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

Organism

Organism	UniProt	Comment	Textmining
Brucella abortus	-	-	-
Escherichia coli	-	-	-
Homo sapiens	-	-	-
Saccharomyces cerevisiae	-	-	-
Salmonella enterica subsp. enterica serovar Typhimurium	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
DNA	mitochondrial lon binds preferentially to single-stranded DNA in a sequence-dependent manner	Homo sapiens	?	-	?
mitochondrial processing peptidase alpha subunit + H2O	human lon initiates substrate cleavage at surface exposed sites, lon degrades mitochondrial processing peptidase alpha subunit only when it is folded	Homo sapiens	?	-	?
ribosomal S2 protein + H2O	major lon cleavages sites within the bacterial S2 ribosomal protein located at the interior of the molecule	Escherichia coli	?	-	?
RNA	mitochondrial lon binds preferentially to single-stranded RNA in a sequence-dependent manner	Homo sapiens	?	-	?
S1 peptide + H2O	decapeptide S1 containing the amino acid residues 89-98 of the bacteriophage lambdaN transcription anti-termination factor, and a fluorescence donor-acceptor pair	Escherichia coli	?	-	?
steroidogenic acute regulatory protein + H2O	human lon initiates substrate cleavage at surface exposed sites	Homo sapiens	?	-	?

Subunits

Subunits	Comment	Organism
heptamer	cryoelectron microscopy	Homo sapiens
heptamer	cryoelectron microscopy	Saccharomyces cerevisiae
hexamer	electron microscopy	Escherichia coli

Synonyms

Synonyms	Comment	Organism
ATP-dependent lon protease	-	Salmonella enterica subsp. enterica serovar Typhimurium
ATP-dependent lon protease	-	Escherichia coli
ATP-dependent lon protease	-	Homo sapiens
ATP-dependent lon protease	-	Saccharomyces cerevisiae
ATP-dependent lon protease	-	Brucella abortus
lon	-	Homo sapiens
lon	-	Saccharomyces cerevisiae
lon protease	-	Salmonella enterica subsp. enterica serovar Typhimurium
lon protease	-	Escherichia coli
lon protease	-	Homo sapiens
lon protease	-	Saccharomyces cerevisiae
lon protease	-	Brucella abortus
Pim1p	-	Saccharomyces cerevisiae
Protease La	-	Salmonella enterica subsp. enterica serovar Typhimurium
Protease La	-	Escherichia coli
Protease La	-	Homo sapiens
Protease La	-	Saccharomyces cerevisiae
Protease La	-	Brucella abortus

Cofactor

Cofactor	Comment	Organism	Structure
ATP	-	Escherichia coli

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Release 2023.1 (January 2023)