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Literature summary for 3.4.21.53 extracted from

  • Menon, A.S.; Goldberg, A.L.
    Binding of nucleotides to the ATP-dependent protease La from Escherichia coli (1987), J. Biol. Chem., 262, 14921-14928.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
Adenyl-5'-yl imidodiphosphate i.e. AMP-PNP, activation Escherichia coli
Adenyl-5'-yl imidodiphosphate competes for one of the ATP-high-affinity binding-sites Escherichia coli
Adenyl-5'-yl imidodiphosphate peptide hydrolysis Escherichia coli
adenyl-5'-yl methylene monophosphonate i.e. AMP-CPP, activation, competes for the two ATP-high affinity sites Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
ADP ADP-binding in the presence of EDTA; kinetics; product inhibition Escherichia coli
vanadate decavanadate (not orthovanadate) Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ requirement Escherichia coli
Mg2+ 10 mM Escherichia coli
Mn2+ requirement, as Mn2+-ATP Escherichia coli
Mn2+ can replace Mg2+-ATP Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
carrying lon-gene on the chromosome
-
Escherichia coli
-
carrying lon-gene on plasmid pJMC40
-

Storage Stability

Storage Stability Organism
-70°C, in 40% glycerol, stable Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
casein + H2O
-
Escherichia coli hydrolyzed casein
-
?
Glutaryl-Ala-Ala-Phe-methoxynaphthylamide + H2O
-
Escherichia coli Glutaryl-Ala-Ala-Phe + methoxynaphthylamine
-
?
Succinyl-Phe-Ala-Phe-methoxynaphthylamide + H2O
-
Escherichia coli Succinyl-Phe-Ala-Phe + methoxynaphthylamine
-
?

Cofactor

Cofactor Comment Organism Structure
ATP requirement Escherichia coli
ATP only phosphate is released after ATP hydrolysis Escherichia coli
ATP ADP remains on the enzyme Escherichia coli
ATP ATP-binding is reversible Escherichia coli
ATP ATP- or ATP-analog-binding in the presence of EDTA Escherichia coli
ATP ATP-dependent protease Escherichia coli
ATP enzyme binds 4 mol ATP per tetramer at ATP concentrations above 0.01 mM Escherichia coli
ATP enzyme binds 2 mol ATP/tetramer in the absence of divalent cations or at 0.01 mM ATP in the presence of Mn2+ or Mg2+ Escherichia coli
ATP diphosphate, adenyl-5'-yl methylene diphosphate, GTP, UTP and CTP at 1 mM have no effect on the binding of ATP to the enzyme Escherichia coli