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Literature summary extracted from

  • Goldberg, A.L.; Waxman, L.
    The role of ATP hydrolysis in the breakdown of proteins and peptides by protease La from Escherichia coli (1985), J. Biol. Chem., 260, 12029-12034.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.4.21.53 adenosine 5'-(3-thiotriphosphate) i.e. adenosine 5'-O-(thiotriphosphate) or ATP-gamma-S, activation Escherichia coli
3.4.21.53 adenosine 5'-(3-thiotriphosphate) hydrolysis, peptide not protein hydrolysis Escherichia coli
3.4.21.53 Adenyl-5'-yl imidodiphosphate casein or glutaryl-Ala-Ala-Phe-methoxynaphthylamide hydrolysis Escherichia coli
3.4.21.53 Adenyl-5'-yl imidodiphosphate no activation of bovine serum albumin hydrolysis Escherichia coli
3.4.21.53 adenyl-5'-yl methylene diphosphonate i.e. AMP-PCP, activation Escherichia coli
3.4.21.53 adenyl-5'-yl methylene diphosphonate casein or glutaryl-Ala-Ala-Phe-methoxynaphthylamide hydrolysis Escherichia coli
3.4.21.53 GTP activation Escherichia coli
3.4.21.53 GTP less efficient than ATP Escherichia coli
3.4.21.53 additional information enzyme hydroylzes proteins and ATP in a coupled process Escherichia coli
3.4.21.53 additional information peptide substrates, e.g. glutaryl-Ala-Phe-Phe methoxynaphthylamide or succinyl-Phe-Leu-Phe methoxynaphthylamide do not support ATP hydrolysis Escherichia coli
3.4.21.53 additional information polyphosphate (n:17) Escherichia coli
3.4.21.53 additional information protein degradation requires nucleoside triphosphate hydrolysis, cleavage of small peptides only requires binding of nucleotides to the enzyme Escherichia coli
3.4.21.53 Protein substrates promotion of ATP hydrolysis Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.21.53 ADP prevents activation by ATP; prevents activation by diphosphate Escherichia coli
3.4.21.53 Glutaryl-Ala-Ala-Phe ATP hydrolysis Escherichia coli
3.4.21.53 Glutaryl-Ala-Ala-Phe-methoxynaphthylamide ATP-hydrolysis Escherichia coli
3.4.21.53 Peptide substrates inhibit ATP hydrolysis, protein substrates promote ATP hydrolysis Escherichia coli
3.4.21.53 Succinyl-Phe-Ala-Phe-methoxynaphthylamide ATP hydrolysis Escherichia coli
3.4.21.53 vanadate ATPase inhibitor; does not inhibit but even stimulates peptide hydrolysis; inhibits protein hydrolysis Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.4.21.53 0.15
-
 diphosphate (+ peptide) Escherichia coli

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.4.21.53 diphosphate activation Escherichia coli
3.4.21.53 diphosphate in the presence of Mg2+, only peptide hydrolysis, not casein or serum albumin hydrolysis Escherichia coli
3.4.21.53 Mg2+ requirement Escherichia coli
3.4.21.53 Mg2+ as Mg2+-ATP Escherichia coli
3.4.21.53 Tetraphosphate activation, only peptide hydrolysis, in the presence of Mg2+ Escherichia coli
3.4.21.53 Triphosphate activation Escherichia coli
3.4.21.53 Triphosphate linear triphosphate and metaphosphate Escherichia coli
3.4.21.53 Triphosphate in the presence of Mg2+ Escherichia coli
3.4.21.53 Triphosphate only peptide hydrolysis, not casein or serum albumin hydrolysis Escherichia coli

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.4.21.53 94000
-
 x * 94000, SDS-PAGE Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
3.4.21.53 Escherichia coli
-
 K-12
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.21.53 casein + H2O methylcasein Escherichia coli hydrolyzed casein
-
 ?
3.4.21.53 casein + H2O methylated alpha-casein Escherichia coli hydrolyzed casein
-
 ?
3.4.21.53 CNBr-fragments of bovine serum albumin + H2O less dependent on ATP hydrolysis Escherichia coli ?
-
 ?
3.4.21.53 Denatured bovine serum albumin + H2O
-
 Escherichia coli ?
-
 ?
3.4.21.53 Globin + H2O
-
 Escherichia coli ?
-
 ?
3.4.21.53 Glucagon + H2O
-
 Escherichia coli Hydrolyzed glucagon
-
 ?
3.4.21.53 Glutaryl-Ala-Ala-Phe-methoxynaphthylamide + H2O
-
 Escherichia coli Glutaryl-Ala-Ala-Phe + methoxynaphthylamine
-
 ?
3.4.21.53 additional information no phosphorylation of enzyme or substrate during ATP hydrolysis Escherichia coli ?
-
 ?
3.4.21.53 Pancreatic polypeptide + H2O
-
 Escherichia coli ?
-
 ?
3.4.21.53 Parathyroid hormone + H2O
-
 Escherichia coli ?
-
 ?
3.4.21.53 Pro-His-Pro-Phe-His-Leu-Leu-Val-Tyr + H2O nonapeptide related to equine angiotensinogen Escherichia coli ?
-
 ?
3.4.21.53 Succinyl-Phe-Ala-Phe-methoxynaphthylamide + H2O
-
 Escherichia coli Succinyl-Phe-Ala-Phe + methoxynaphthylamine
-
 ?

Subunits

EC Number Subunits Comment Organism
3.4.21.53 multimer x * 94000, SDS-PAGE Escherichia coli

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.4.21.53 37
-
 assay at Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
3.4.21.53 ATP binds to enzyme as allosteric activator allowing peptide bond hydrolysis with subsequent ATP hydrolysis Escherichia coli
3.4.21.53 ATP activation only in the presence of Mg2+ Escherichia coli
3.4.21.53 ATP MgATP2- rather than ATP4- Escherichia coli
3.4.21.53 ATP splitting of high-energy bond of ATP is required for protein breakdown Escherichia coli
3.4.21.53 ATP ATP-dependent protease Escherichia coli
3.4.21.53 ATP ATP hydrolysis is essential for hydrolysis of proteins Escherichia coli
3.4.21.53 ATP ATP hydrolysis is not essential for hydrolysis of peptides Escherichia coli
3.4.21.53 CTP activation Escherichia coli
3.4.21.53 CTP less efficient than ATP Escherichia coli
3.4.21.53 dATP activation Escherichia coli
3.4.21.53 dATP can replace ATP Escherichia coli
3.4.21.53 UTP activation Escherichia coli
3.4.21.53 UTP less efficient than ATP Escherichia coli