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Literature summary for 3.4.21.53 extracted from

  • Vineyard, D.; Patterson-Ward, J.; Lee, I.
    Single-turnover kinetic experiments confirm the existence of high- and low-affinity ATPase sites in Escherichia coli Lon protease (2006), Biochemistry, 45, 4602-4610.
    View publication on PubMedView publication on EuropePMC

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
67000
-
limited tryptic digestion Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O high-affinity sites hydrolyze ATP very slowly, but support multiple rounds of peptide hydrolysis, while the low-affinity sites hydrolyze ATP quickly. Affinities of sites differ from one another 10fold. Hydrolysis at both the high- and low-affinity sites are necessary for optimal peptide cleavage and the stabilization of the conformational change associated with nucleotide binding Escherichia coli phosphate + ADP
-
?
casein + H2O
-
Escherichia coli ?
-
?
YRGITCSGRQK(benzoic acid amide) + H2O
-
Escherichia coli ?
-
?

Synonyms

Synonyms Comment Organism
lon
-
Escherichia coli
lon protease
-
Escherichia coli

Cofactor

Cofactor Comment Organism Structure
ATP best activator of the peptidase activity Escherichia coli
additional information adenylyl 5-imidodiphosphate, can replace ATP, shows a reduced peptidase activity Escherichia coli