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Literature summary for 3.4.21.53 extracted from

  • Fischer, H.; Glockshuber, R.
    ATP hydrolysis is not stoichiometrically linked with proteolysis in the ATP-dependent protease La from Escherichia coli (1993), J. Biol. Chem., 268, 22502-22507.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
Dimethylsulfoxide activation Escherichia coli
Polyethylene glycol activation Escherichia coli
Tween 20 activation Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
wild-type strain W3110 and mutant strain
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Glutaryl-Ala-Ala-Phe-methoxynaphthylamide + H2O
-
Escherichia coli Glutaryl-Ala-Ala-Phe + methoxynaphthylamine
-
?
additional information with a proteolytic and an ATP-binding site per monomer Escherichia coli ?
-
?

Temperature Optimum [°C]

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

Cofactor

Cofactor Comment Organism Structure
ATP proteolytically inactive mutant enzyme with completely unaffected ATPase activity Escherichia coli
ATP ATP-dependent protease Escherichia coli
ATP ATP hydrolysis is not stoichiometrically linked with proteolysis Escherichia coli