Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.4.21.53 extracted from

  • Larimore, F.S.; Waxman, L.; Goldberg, A.L.
    Studies of the ATP-dependent proteolytic enzyme, protease La, from Escherichia coli (1982), J. Biol. Chem., 257, 4187-4195.
    View publication on PubMed
Search for more literature for 3.4.21.53

Activating Compound

Activating Compound Comment Organism Structure
GTP activation Escherichia coli
GTP less efficient than ATP Escherichia coli
additional information ATP cannot be replaced by ADP, AMP Escherichia coli

General Stability

General Stability Organism
ADP and AMP bind to and stabilize the enzyme even in the absence of Mg2+ Escherichia coli
ATP stabilizes Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
2',3'-dialdehyde-ATP i.e. adenosine 2',3'-dialdehyde triphosphate, in the presence of ATP, globin as substrate Escherichia coli
adenosine 5'-(3-thiotriphosphate) i.e. ATP-gamma-S, in the presence of ATP, globin as substrate Escherichia coli
ADP prevents activation by ATP Escherichia coli
alpha,beta-methylene-ATP in the presence of ATP, globin as substrate Escherichia coli
AMP in the presence of ATP Escherichia coli
beta,gamma-methylene-ATP in the presence of ATP, globin as substrate Escherichia coli
Dio-9 ATPase inhibitor Escherichia coli
ethanol
-
 Escherichia coli
KCl weak, above 0.2 M Escherichia coli
additional information termination factor rho or NaN3 Escherichia coli
N,N'-dicyclohexylcarbodiimide not Escherichia coli
NaCl weak, above 0.2 M Escherichia coli
oligomycin weak Escherichia coli
phosphate above 0.1 M Escherichia coli
quercetin
-
 Escherichia coli
vanadate
-
 Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.25
-
 ATP
-
 Escherichia coli

Localization

Localization Comment Organism GeneOntology No. Textmining
soluble
-
 Escherichia coli
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ can replace Mg2+-ATP Escherichia coli
Ca2+ activation, as Ca2+-ATP Escherichia coli
Ca2+ slightly less effective than Mg2+-ATP Escherichia coli
diphosphate not Escherichia coli
Mg2+ requirement Escherichia coli
Mg2+ as Mg2+-ATP Escherichia coli
Mn2+ requirement, as Mn2+-ATP Escherichia coli
Mn2+ slightly more effective than Mg2+-ATP Escherichia coli
Mn2+ can replace Mg2+-ATP Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
 K-12
-

Purification (Commentary)

Purification (Comment) Organism
partial Escherichia coli

Storage Stability

Storage Stability Organism
4°C, about 60% loss of activity within 4 days, 3 mM ATP stabilizes Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O
-
 Escherichia coli phosphate + ADP
-
 ?
casein + H2O alpha-casein Escherichia coli hydrolyzed casein
-
 ?
casein + H2O methylcasein Escherichia coli hydrolyzed casein
-
 ?
Globin + H2O
-
 Escherichia coli ?
-
 ?
Methylglobin + H2O methyl-apohemoglobin Escherichia coli ?
-
 ?

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
42
-
 1 h, 80% loss of activity, 3 mM ATP stabilizes, ADP or AMP less effectively, not Mg2+ Escherichia coli

Cofactor

Cofactor Comment Organism Structure
ATP requirement Escherichia coli
ATP activation only in the presence of Mg2+ Escherichia coli
ATP MgATP2- rather than ATP4- Escherichia coli
ATP ATP-dependent protease Escherichia coli
ATP MnATP2- or CaATP2- rather than ATP4- Escherichia coli
ATP rapid depletion of ATP prevents proteolysis Escherichia coli
CTP activation Escherichia coli
CTP less efficient than ATP Escherichia coli
dATP activation Escherichia coli
dATP supports proteolysis with 75% the efficiency of ATP Escherichia coli
UTP activation Escherichia coli
UTP less efficient than ATP Escherichia coli