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

BRENDA support

Literature summary for 3.4.21.53 extracted from

  • Waxman, L.; Goldberg, A.L.
    Protease La, the lon gene product, cleaves specific fluorogenic peptides in an ATP-dependent reaction (1985), J. Biol. Chem., 260, 12022-12028.
    View publication on PubMed
Search for more literature for 3.4.21.53

Activating Compound

Activating Compound Comment Organism Structure
Denatured calf thymus or E. coli DNA stimulation of glutaryl-Ala-Ala-Phe-methoxynaphthylamide hydrolysis Escherichia coli
additional information no activation by benzoyl-Arg-Gly-Phe-Phe-Leu methoxynaphthylamide (glutaryl-Ala-Ala-Phe methoxynaphthylamide as substrate), poly(A) Escherichia coli
additional information ATP cannot be replaced by ADP, AMP Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
Acetyl-Gly-Gly-Ala chloromethyl ketone
-
 Escherichia coli
ADP prevents activation by ATP; strong Escherichia coli
Ala-Lys-Arg chloromethyl ketone weak, casein as substrate Escherichia coli
AMP not Escherichia coli
Benzoyl-Arg-Gly-Phe-methoxynaphthylamide
-
 Escherichia coli
Benzoyl-Arg-Gly-Phe-Phe-Leu-methoxynaphthylamide glutaryl-Ala-Ala-Phe-methoxynaphthylamide or casein as substrate Escherichia coli
benzyloxycarbonyl-Gly-Leu-Phe chloromethyl ketone strong Escherichia coli
benzyloxycarbonyl-Gly-Leu-Pro chloromethyl ketone
-
 Escherichia coli
Benzyloxycarbonyl-Gly-NH-C6H4SO2-Phe weak Escherichia coli
benzyloxycarbonyl-Phe chloromethyl ketone weak Escherichia coli
chymostatin weak Escherichia coli
diisopropyl fluorophosphate
-
 Escherichia coli
dimethylformamide above 5% Escherichia coli
Dimethylsulfoxide above 5% Escherichia coli
Glutaryl-Ala-Ala-Phe-methoxynaphthylamide weak, casein as substrate Escherichia coli
heparin strong Escherichia coli
Isopropanol above 5% Escherichia coli
additional information methoxynaphthylamide (ATP-hydrolysis) Escherichia coli
N-ethylmaleimide
-
 Escherichia coli
p-nitroanthranilate weak Escherichia coli
PMSF
-
 Escherichia coli
Protein R9 from Escherichia coli mutant strain capR9 protein, peptide and ATP hydrolysis Escherichia coli
tosyl-Lys chloromethyl ketone i.e. 1-chloro-3-tosylamido-2-heptanone; weak, casein as substrate, no inhibition with glutaryl-Ala-Ala-Phe methoxynaphthylamide as substrate Escherichia coli
tosyl-Phe chloromethyl ketone i.e. tosyl-2-phenylethyl chloromethyl ketone Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.003 0.005 ATP cosubstrate glutaryl-Ala-Ala-Phe-methoxynaphthylamide Escherichia coli
0.4 0.5 Glutaryl-Ala-Ala-Phe-methoxynaphthylamide
-
 Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ with equal efficiency in peptide hydrolysis (not protein hydrolysis) Escherichia coli
Ca2+ can replace Mg2+-ATP Escherichia coli
Ca2+ activation, as Ca2+-ATP Escherichia coli
Mg2+ requirement Escherichia coli
Mg2+ as Mg2+-ATP Escherichia coli
Mg2+ Mg2+ alone much less effective Escherichia coli
Mn2+ requirement, as Mn2+-ATP Escherichia coli
Mn2+ only weak activity with Mn2+ alone Escherichia coli
Mn2+ with equal efficiency in peptide hydrolysis (not protein hydrolysis) Escherichia coli
Mn2+ can replace Mg2+-ATP Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Storage Stability

Storage Stability Organism
-70°C, apparent stimulation by ATP falls by 60% after prolonged storage Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O
-
 Escherichia coli phosphate + ADP
-
 ?
casein + H2O methylcasein Escherichia coli hydrolyzed casein
-
 ?
Denatured bovine serum albumin + H2O
-
 Escherichia coli ?
-
 ?
Fluorogenic peptides + H2O
-
 Escherichia coli ?
-
 ?
Glutaryl-Ala-Ala-Ala-methoxynaphthylamide + H2O hydrolyzed at 3-4% the rate of glutaryl-Ala-Ala-Phe-methoxynaphthylamide Escherichia coli Glutaryl-Ala-Ala-Ala + methoxynaphthylamine
-
 ?
Glutaryl-Ala-Ala-Phe-methoxynaphthylamide + H2O fluorogenic peptide, 0.3 mM Escherichia coli Glutaryl-Ala-Ala-Phe + methoxynaphthylamine
-
 ?
Glutaryl-Gly-Gly-Pro-methoxynaphthylamide + H2O hydrolyzed at 6% the rate of glutaryl-Ala-Ala-Phe-methoxynaphthylamide Escherichia coli Glutaryl-Gly-Gly-Pro + methoxynaphthylamine
-
 ?
additional information No substrates are glutaryl-Phe-7-amino-4-methylcoumarin, Ala-Ala-Phe-methoxynaphthylamide, Gly-Phe-methoxynaphthylamide, Asp-methoxynaphthylamide, Leu-methoxynaphthylamide, Arg-methoxynaphthylamide, Ala-methoxynaphthylamide, Tyr-methoxynaphthylamide, Lys-methoxynaphthylamide, methoxyglutaryl-Ala-Ala-Phe-methoxynaphthylamide, methoxysuccinyl-Ala-Ala-Phe-methoxynaphthylamide, benzyloxycarbonyl-Ala-Pro-methoxynaphthylamide, benzoyl-Arg-Gly-Phe-Phe-Leu-methoxynaphthylamide, benzoyl-Arg-Gly-Leu-methoxynaphthylamide, Leu-Gly-Gly-methoxynaphthylamide, Ser-Tyr-methoxynaphthylamide Escherichia coli ?
-
 ?
Succinyl-Ala-Ala-Phe-methoxynaphthylamide + H2O best substrate Escherichia coli Succinyl-Ala-Ala-Phe + methoxynaphthylamine
-
 ?
Succinyl-Phe-Ala-Phe-methoxynaphthylamide + H2O fluorogenic peptide, hydrolyzed at 75% the rate of glutaryl-Ala-Ala-Phe-methoxynaphthylamide Escherichia coli Succinyl-Phe-Ala-Phe + methoxynaphthylamine
-
 ?

Temperature Optimum [°C]

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

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
9 9.5
-
 Escherichia coli

Cofactor

Cofactor Comment Organism Structure
ATP effect of enzyme purification or storage on stimulation by ATP 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