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Literature summary for 3.4.21.53 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

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

Inhibitors

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

KM Value [mM]

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

Metals/Ions

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

Molecular Weight [Da]

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

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
K-12
-

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
multimer x * 94000, SDS-PAGE 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 binds to enzyme as allosteric activator allowing peptide bond hydrolysis with subsequent ATP hydrolysis Escherichia coli
ATP activation only in the presence of Mg2+ Escherichia coli
ATP MgATP2- rather than ATP4- Escherichia coli
ATP splitting of high-energy bond of ATP is required for protein breakdown Escherichia coli
ATP ATP-dependent protease Escherichia coli
ATP ATP hydrolysis is essential for hydrolysis of proteins Escherichia coli
ATP ATP hydrolysis is not essential for hydrolysis of peptides Escherichia coli
CTP activation Escherichia coli
CTP less efficient than ATP Escherichia coli
dATP activation Escherichia coli
dATP can replace ATP Escherichia coli
UTP activation Escherichia coli
UTP less efficient than ATP Escherichia coli